The American Journal of Holistic heart wellness Body fat calipers for professionals, 99 2— Protein for weight loss in athletes Weighf rates of muscle protein turnover Proteni amino acid transport after resistance exercise in humans. Stoll B, Burrin DG. Abstract There exists a large body of scientific evidence to support protein intakes in excess of the recommended dietary allowance RDA 0.

Protein for weight loss in athletes -

Research indicates that rates of MPS rapidly rise to peak levels within 30 min of protein ingestion and are maintained for up to three hours before rapidly beginning to lower to basal rates of MPS even though amino acids are still elevated in the blood [ ].

Using an oral ingestion model of 48 g of whey protein in healthy young men, rates of myofibrillar protein synthesis increased three-fold within 45—90 min before slowly declining to basal rates of MPS all while plasma concentration of EAAs remained significantly elevated [ ].

While largely unexplored in a human model, these authors relied upon an animal model and were able to reinstate increases in MPS using the consumption of leucine and carbohydrate min after ingestion of the first meal.

As such, it is suggested that individuals attempting to restrict caloric intake should consume three to four whole meals consisting of 20—40 g of protein per meal. While this recommendation stems primarily from initial work that indicated protein doses of 20—40 g favorably promote increased rates of MPS [ 31 , , ], Kim and colleagues [ ] recently reported that a 70 g dose of protein promoted a more favorable net balance of protein when compared to a 40 g dose due to a stronger attenuation of rates of muscle protein breakdown.

For those attempting to increase their calories, we suggest consuming small snacks between meals consisting of both a complete protein and a carbohydrate source. This contention is supported by research from Paddon-Jones et al. These researchers compared three cal mixed macronutrient meals to three cal meals combined with three cal amino acid-carbohydrate snacks between meals.

Additionally, using a protein distribution pattern of 20—25 g doses every three hours in response to a single bout of lower body resistance exercise appears to promote the greatest increase in MPS rates and phosphorylation of key intramuscular proteins linked to muscle hypertrophy [ ]. This simple addition could provide benefits for individuals looking to increase muscle mass and improve body composition in general while also striving to maintain or improve health and performance.

The current RDA for protein is 0. While previous recommendations have suggested a daily intake of 1. Daily and per dose needs are combinations of many factors including volume of exercise, age, body composition, total energy intake and training status of the athlete.

Daily intakes of 1. Even higher amounts ~70 g appear to be necessary to promote attenuation of muscle protein breakdown. Pacing or spreading these feeding episodes approximately three hours apart has been consistently reported to promote sustained, increased levels of MPS and performance benefits.

There are 20 total amino acids, comprised of 9 EAAs and 11 non-essential amino acids NEAAs. EAAs cannot be produced in the body and therefore must be consumed in the diet. Several methods exist to determine protein quality such as Chemical Score, Protein Efficiency Ratio, Biological Value, Protein Digestibility-Corrected Amino Acid Score PDCAAS and most recently, the Indicator Amino Acid Oxidation IAAO technique.

Ultimately, in vivo protein quality is typically defined as how effective a protein is at stimulating MPS and promoting muscle hypertrophy [ ]. Overall, research has shown that products containing animal and dairy-based proteins contain the highest percentage of EAAs and result in greater hypertrophy and protein synthesis following resistance training when compared to a vegetarian protein-matched control, which typically lacks one or more EAAs [ 86 , 93 , ].

Several studies, but not all, [ ] have indicated that EAAs alone stimulate protein synthesis in the same magnitude as a whole protein with the same EAA content [ 98 ]. For example, Borsheim et al. Moreover, Paddon-Jones and colleagues [ 96 ] found that a cal supplement containing 15 g of EAAs stimulated greater rates of protein synthesis than an cal meal with the same EAA content from a whole protein source.

While important, the impact of a larger meal on changes in circulation and the subsequent delivery of the relevant amino acids to the muscle might operate as important considerations when interpreting this data.

In contrast, Katsanos and colleagues [ ] had 15 elderly subjects consume either 15 g of whey protein or individual doses of the essential and nonessential amino acids that were identical to what is found in a g whey protein dose on separate occasions.

Whey protein ingestion significantly increased leg phenylalanine balance, an index of muscle protein accrual, while EAA and NEAA ingestion exerted no significant impact on leg phenylalanine balance.

This study, and the results reported by others [ ] have led to the suggestion that an approximate 10 g dose of EAAs might serve as an optimal dose to maximally stimulate MPS and that intact protein feedings of appropriate amounts as opposed to free amino acids to elderly individuals may stimulate greater improvements in leg muscle protein accrual.

Based on this research, scientists have also attempted to determine which of the EAAs are primarily responsible for modulating protein balance. The three branched-chain amino acids BCAAs , leucine, isoleucine, and valine are unique among the EAAs for their roles in protein metabolism [ ], neural function [ , , ], and blood glucose and insulin regulation [ ].

Additionally, enzymes responsible for the degradation of BCAAs operate in a rate-limiting fashion and are found in low levels in splanchnic tissues [ ].

Thus, orally ingested BCAAs appear rapidly in the bloodstream and expose muscle to high concentrations ultimately making them key components of skeletal MPS [ ]. Furthermore, Wilson and colleagues [ ] have recently demonstrated, in an animal model, that leucine ingestion alone and with carbohydrate consumed between meals min post-consumption extends protein synthesis by increasing the energy status of the muscle fiber.

Multiple human studies have supported the contention that leucine drives protein synthesis [ , ]. Moreover, this response may occur in a dose-dependent fashion, plateauing at approximately two g at rest [ 31 , ], and increasing up to 3. However, it is important to realize that the duration of protein synthesis after resistance exercise appears to be limited by both the signal leucine concentrations , ATP status, as well as the availability of substrate i.

As such, increasing leucine concentration may stimulate increases in muscle protein, but a higher total dose of all EAAs as free form amino acids or intact protein sources seems to be most suited for sustaining the increased rates of MPS [ ].

It is well known that exercise improves net muscle protein balance and in the absence of protein feeding, this balance becomes more negative.

When combined with protein feeding, net muscle protein balance after exercise becomes positive [ ]. Norton and Layman [ ] proposed that consumption of leucine, could turn a negative protein balance to a positive balance following an intense exercise bout by prolonging the MPS response to feeding.

In support, the ingestion of a protein or essential amino acid complex that contains sufficient amounts of leucine has been shown to shift protein balance to a net positive state after intense exercise training [ 46 , ]. Even though leucine has been demonstrated to independently stimulate protein synthesis, it is important to recognize that supplementation should not be with just leucine alone.

For instance, Wilson et al. In summary, athletes should focus on consuming adequate leucine content in each of their meals through selection of high-quality protein sources [ ]. Protein sources containing higher levels of the EAAs are considered to be higher quality sources of protein.

The body uses 20 amino acids to make proteins, seven of which are essential nine conditionally , requiring their ingestion to meet daily needs.

EAAs appear to be uniquely responsible for increasing MPS with doses ranging from 6 to 15 g all exerting stimulatory effects. In addition, doses of approximately one to three g of leucine per meal appear to be needed to stimulate protein translation machinery.

The BCAAs i. However, the extent to which these changes are aligned with changes in MPS remains to be fully explored. While greater doses of leucine have been shown to independently stimulate increases in protein synthesis, a balanced consumption of the EAAs promotes the greatest increases.

Milk proteins have undergone extensive research related to their potential roles in augmenting adaptations from exercise training [ 86 , 93 ].

For example, consuming milk following exercise has been demonstrated to accelerate recovery from muscle damaging exercise [ ], increase glycogen replenishment [ ], improve hydration status [ , ], and improve protein balance to favor synthesis [ 86 , 93 ], ultimately resulting in increased gains in both neuromuscular strength and skeletal muscle hypertrophy [ 93 ].

Moreover, milk protein contains the highest score on the PDCAAS rating system, and in general contains the greatest density of leucine [ ]. Milk can be fractionated into two protein classes, casein and whey. While both are high in quality, the two differ in the rate at which they digest as well as the impact they have on protein metabolism [ , , ].

Whey protein is water soluble, mixes easily, and is rapidly digested [ ]. In contrast, casein is water insoluble, coagulates in the gut and is digested more slowly than whey protein [ ].

Casein also has intrinsic properties such as opioid peptides, which effectively slow gastric motility [ ]. Original research investigating the effects of digestion rate was conducted by Boirie, Dangin and colleagues [ , , ].

These researchers gave a 30 g bolus of whey protein and a 43 g bolus of casein protein to subjects on separate occasions and measured amino acid levels for several hours after ingestion.

They reported that the whey protein condition displayed robust hyperaminoacidemia min after administration. However, by min, amino acid concentrations had returned to baseline. In contrast, the casein condition resulted in a slow increase in amino acid concentrations, which remained elevated above baseline after min.

Over the study duration, casein produced a greater whole body leucine balance than the whey protein condition, leading the researcher to suggest that prolonged, moderate hyperaminoacidemia is more effective at stimulating increases in whole body protein anabolism than a robust, short lasting hyperaminoacidemia.

While this research appears to support the efficacy of slower digesting proteins, subsequent work has questioned its validity in athletes. The first major criticism is that Boire and colleagues investigated whole body non-muscle and muscle protein balance instead of skeletal myofibrillar MPS.

These findings suggest that changes in whole body protein turnover may poorly reflect the level of skeletal muscle protein metabolism that may be taking place. Trommelen and investigators [ ] examined 24 young men ingesting 30 g of casein protein with or without completion of a single bout of resistance exercise, and concluded that rates of MPS were increased, but whole-body protein synthesis rates were not impacted.

More recently, Tang and colleagues [ 86 ] investigated the effects of administering 22 g of hydrolyzed whey isolate and micellar casein 10 g of EAAs at both rest and following a single bout of resistance training in young males. Moreover, these researchers reported that whey protein ingestion stimulated greater MPS at both rest and following exercise when compared to casein.

In comparison to the control group, both whey and casein significantly increased leucine balance, but no differences were found between the two protein sources for amino acid uptake and muscle protein balance. Additional research has also demonstrated that 10 weeks of whey protein supplementation in trained bodybuilders resulted in greater gains in lean mass 5.

These findings suggest that the faster-digesting whey proteins may be more beneficial for skeletal muscle adaptations than the slower digesting casein.

Skeletal muscle glycogen stores are a critical element to both prolonged and high-intensity exercise. In skeletal muscle, glycogen synthase activity is considered one of the key regulatory factors for glycogen synthesis. Research has demonstrated that the addition of protein in the form of milk and whey protein isolate 0.

Further, the addition of protein facilitates repair and recovery of the exercised muscle [ 12 ]. These effects are thought to be related to a greater insulin response following the exercise bout. Intriguingly, it has also been demonstrated that whey protein enhances glycogen synthesis in the liver and skeletal muscle more than casein in an insulin-independent fashion that appears to be due to its capacity to upregulate glycogen synthase activity [ ].

Therefore, the addition of milk protein to a post-workout meal may augment recovery, improve protein balance, and speed glycogen replenishment.

While athletes tend to view whey as the ideal protein for skeletal muscle repair and function it also has several health benefits. In particular, whey protein contains an array of biologically active peptides whose amino acids sequences give them specific signaling effects when liberated in the gut.

Furthermore, whey protein appears to play a role in enhancing lymphatic and immune system responses [ ]. In addition, α-lactalbumin contains an ample supply of tryptophan which increases cognitive performance under stress [ ], improves the quality of sleep [ , ], and may also speed wound healing [ ], properties which could be vital for recovery from combat and contact sporting events.

In addition, lactoferrin is also found in both milk and in whey protein, and has been demonstrated to have antibacterial, antiviral, and antioxidant properties [ ]. Moreover, there is some evidence that whey protein can bind iron and therefore increase its absorption and retention [ ]. Egg protein is often thought of as an ideal protein because its amino acid profile has been used as the standard for comparing other dietary proteins [ ].

Due to their excellent digestibility and amino acid content, eggs are an excellent source of protein for athletes. While the consumption of eggs has been criticized due to their cholesterol content, a growing body of evidence demonstrates the lack of a relationship between egg consumption and coronary heart disease, making egg-based products more appealing [ ].

One large egg has 75 kcal and 6 g of protein, but only 1. Research using eggs as the protein source for athletic performance and body composition is lacking, perhaps due to less funding opportunities relative to funding for dairy. Egg protein may be particularly important for athletes, as this protein source has been demonstrated to significantly increase protein synthesis of both skeletal muscle and plasma proteins after resistance exercise at both 20 and 40 g doses.

Leucine oxidation rates were found to increase following the 40 g dose, suggesting that this amount exceeds an optimal dose [ 31 ]. In addition to providing a cost effective, high-quality source of protein rich in leucine 0.

Functional foods are defined as foods that, by the presence of physiologically active components, provide a health benefit beyond basic nutrition [ ]. According to the Academy of Nutrition and Dietetics, functional foods should be consumed as part of a varied diet on a regular basis, at effective levels [ ].

Thus, it is essential that athletes select foods that meet protein requirements and also optimize health and prevent decrements in immune function following intense training. Eggs are also rich in choline, a nutrient which may have positive effects on cognitive function [ ].

Moreover, eggs provide an excellent source of the carotenoid-based antioxidants lutein and zeaxanthin [ ]. Also, eggs can be prepared with most meal choices, whether at breakfast, lunch, or dinner.

Such positive properties increase the probability of the athletes adhering to a diet rich in egg protein. Meat proteins are a major staple in the American diet and, depending on the cut of meat, contain varying amounts of fat and cholesterol.

Meat proteins are well known to be rich sources of the EAAs [ ]. Beef is a common source of dietary protein and is considered to be of high biological value because it contains the full balance of EAAs in a fraction similar to that found in human skeletal muscle [ ].

A standard serving of Moreover, this 30 g dose of beef protein has been shown to stimulate protein synthesis in both young and elderly subjects [ ]. In addition to its rich content of amino acids, beef and other flesh proteins can serve as important sources of micronutrients such as iron, selenium, vitamins A, B12 and folic acid.

This is a particularly important consideration for pregnant and breastfeeding women. Ultimately, as an essential part of a mixed diet, meat helps to ensure adequate distribution of essential micronutrients and amino acids to the body. Research has shown that significant differences in skeletal muscle mass and body composition between older men who resistance train and either consume meat-based or lactoovovegetarian diet [ ].

Over a week period, whole-body density, fat-free mass, and whole-body muscle mass as measured by urinary creatinine excretion increased in the meat-sourced diet group but decreased in the lactoovovegetarian diet group.

These results indicate that not only do meat-based diets increase fat-free mass, but also they may specifically increase muscle mass, thus supporting the many benefits of meat-based diets. A diet high in meat protein in older adults may provide an important resource in reducing the risk of sarcopenia.

Positive results have also been seen in elite athletes that consume meat-based proteins, as opposed to vegetarian diets [ ]. For example, carnitine is a molecule that transports long-chain fatty acids into mitochondria for oxidation and is found in high amounts in meat.

While evidence is lacking to support an increase in fat oxidation with increased carnitine availability, carnitine has been linked to the sparing of muscle glycogen, and decreases in exercise-induced muscle damage [ ].

Certainly, more research is needed to support these assertions. Creatine is a naturally occurring compound found mainly in muscle. Vegetarians have lower total body creatine stores than omnivores, which demonstrates that regular meat eating has a significant effect on human creatine status [ ].

Moreover, creatine supplementation studies with vegetarians indicate that increased creatine uptake levels do exist in people who practice various forms of vegetarianism [ ].

Sharp and investigators [ ] published the only study known to compare different supplemental powdered forms of animal proteins on adaptations to resistance training such as increases in strength and improvements in body composition. Forty-one men and women performed a standardized resistance-training program over eight weeks and consumed a daily 46 g dose of either hydrolyzed chicken protein, beef protein isolate, or whey protein concentrate in comparison to a control group.

All groups experienced similar increases in upper and lower-body strength, but all protein-supplemented groups reported significant increases in lean mass and decreases in fat mass. Meat-based diets have been shown to include additional overall health benefits.

Some studies have found that meat, as a protein source, is associated with higher serum levels of IGF-1 [ ], which in turn is related to increased bone mineralization and fewer fractures [ ].

A highly debated topic in nutrition and epidemiology is whether vegetarian diets are a healthier choice than omnivorous diets. One key difference is the fact that vegetarian diets often lack equivalent amounts of protein when compared to omnivorous diets [ ].

However, with proper supplementation and careful nutritional choices, it is possible to have complete proteins in a vegetarian diet. Generally by consuming high-quality, animal-based products meat, milk, eggs, and cheese an individual will achieve optimal growth as compared to ingesting only plant proteins [ ].

Research has shown that soy is considered a lower quality complete protein. Hartman et al. They found that the participants that consumed the milk protein increased lean mass and decreased fat mass more than the control and soy groups. Moreover, the soy group was not significantly different from the control group.

Similarly, a study by Tang and colleagues [ 86 ] directly compared the abilities of hydrolyzed whey isolate, soy isolate, and micellar casein to stimulate rates of MPS both at rest and in response to a single bout of lower body resistance training. These authors reported that the ability of soy to stimulate MPS was greater than casein, but less than whey, at rest and in response to an acute resistance exercise stimulus.

While soy is considered a complete protein, it contains lower amounts of BCAAs than bovine milk [ ]. Additionally, research has found that dietary soy phytoestrogens inhibit mTOR expression in skeletal muscle through activation of AMPK [ ].

Thus, not only does soy contain lower amounts of the EAAs and leucine, but soy protein may also be responsible for inhibiting growth factors and protein synthesis via its negative regulation of mTOR.

When considering the multitude of plant sources of protein, soy overwhelmingly has the most research. Limited evidence using wheat protein in older men has suggested that wheat protein stimulates significantly lower levels of MPS when compared to an identical dose 35 g of casein protein, but when this dose is increased nearly two fold 60 g this protein source is able to significantly increase rates of myofibrillar protein synthesis [ ].

As mentioned earlier, a study by Joy and colleagues [ 89 ] in which participants participated in resistance training program for eight weeks while taking identical, high doses of either rice or whey protein, demonstrated that rice protein stimulated similar increases in body composition adaptations to whey protein.

The majority of available science has explored the efficacy of ingesting single protein sources, but evidence continues to mount that combining protein sources may afford additional benefits [ ]. For example, a week resistance training study by Kerksick and colleagues [ 22 ] demonstrated that a combination of whey 40 g and casein 8 g yielded the greatest increase in fat-free mass determined by DEXA when compared to both a combination of 40 g of whey, 5 g of glutamine, and 3 g of BCAAs and a placebo consisting of 48 g of a maltodextrin carbohydrate.

Later, Kerksick et al. Similarly, Hartman and investigators [ 93 ] had 56 healthy young men train for 12 weeks while either ingesting isocaloric and isonitrogenous doses of fat-free milk a blend of whey and casein , soy protein or a carbohydrate placebo and concluded that fat-free milk stimulated the greatest increases in Type I and II muscle fiber area as well as fat-free mass; however, strength outcomes were not affected.

Moreover, Wilkinson and colleagues [ 94 ] demonstrated that ingestion of fat-free milk vs. soy or carbohydrate led to a greater area under the curve for net balance of protein and that the fractional synthesis rate of muscle protein was greatest after milk ingestion.

In , Reidy et al. However, when the entire four-hour measurement period was considered, no difference in MPS rates were found. A follow-up publication from the same clinical trial also reported that ingestion of the protein blend resulted in a positive and prolonged amino acid balance when compared to ingestion of whey protein alone, while post-exercise rates of myofibrillar protein synthesis were similar between the two conditions [ ].

Reidy et al. No differences were found between whey and the whey and soy blend. Some valid criteria exist to compare protein sources and provide an objective method of how to include them in a diet. As previously mentioned, common means of assessing protein quality include Biological Value, Protein Efficiency Ratio, PDCAAS and IAAO.

The derivation of each technique is different with all having distinct advantages and disadvantages. For nearly all populations, ideal methods should be linked to the capacity of the protein to positively affect protein balance in the short term, and facilitate increases and decreases in lean and fat-mass, respectively, over the long term.

To this point, dairy, egg, meat, and plant-based proteins have been discussed. As mentioned previously, initial research by Boirie and Dangin has highlighted the impact of protein digestion rate on net protein balance with the two milk proteins: whey and casein [ , , ].

Subsequent follow-up work has used this premise as a reference point for the digestion rates of other protein sources. Using the criteria of leucine content, Norton and Wilson et al.

Wheat and soy did not stimulate MPS above fasted levels, whereas egg and whey proteins significantly increased MPS rates, with MPS for whey protein being greater than egg protein. MPS responses were closely related to changes in plasma leucine and phosphorylation of 4E—BP1 and S6 K protein signaling molecules.

More importantly, following 2- and weeks of ingestion, it was demonstrated that the leucine content of the meals increased muscle mass and was inversely correlated with body fat. Tang et al. These findings lead us to conclude that athletes should seek protein sources that are both fast-digesting and high in leucine content to maximally stimulate rates of MPS at rest and following training.

Moreover, in consideration of the various additional attributes that high-quality protein sources deliver, it may be advantageous to consume a combination of higher quality protein sources dairy, egg, and meat sources. Multiple protein sources are available for an athlete to consider, and each has their own advantages and disadvantages.

Protein sources are commonly evaluated based upon the content of amino acids, particularly the EAAs, they provide. Blends of protein sources might afford a favorable combination of key nutrients such as leucine, EAAs, bioactive peptides, and antioxidants, but more research is needed to determine their ideal composition.

Nutrient density is defined as the amount of a particular nutrient carbohydrate, protein, fat, etc. per unit of energy in a given food.

In many situations, the commercial preparation method of foods can affect the actual nutrient density of the resulting food. When producing milk protein supplements, special preparations must be made to separate the protein sources from the lactose and fat calories in milk. For example, the addition of acid to milk causes the casein to coagulate or collect at the bottom, while the whey is left on the top [ ].

These proteins are then filtered to increase their purity. Filtration methods differ, and there are both benefits and disadvantages to each. Ion exchange exposes a given protein source, such as whey, to hydrochloric acid and sodium hydroxide, thereby producing an electric charge on the proteins that can be used to separate them from lactose and fat [ ].

The advantage of this method is that it is relatively cheap and produces the highest protein concentration [ ]. The disadvantage is that ion exchange filtration typically denatures some of the valuable immune-boosting, anti-carcinogenic peptides found in whey [ ].

Cross-flow microfiltration, and ultra-micro filtration are based on the premise that the molecular weight of whey protein is greater than lactose, and use 1 and 0.

As a result, whey protein is trapped in the membranes but the lactose and other components pass through. The advantage is that these processes do not denature valuable proteins and peptides found in whey, so the protein itself is deemed to be of higher quality [ ].

The main disadvantage is that this filtration process is typically costlier than the ion exchange method. When consumed whole, proteins are digested through a series of steps beginning with homogenization by chewing, followed by partial digestion by pepsin in the stomach [ ]. Following this, a combination of peptides, proteins, and negligible amounts of single amino acids are released into the small intestine and from there are either partially hydrolyzed into oligopeptides, 2—8 amino acids in length or are fully hydrolyzed into individual amino acids [ ].

Absorption of individual amino acids and various small peptides di, tri, and tetra into the blood occurs inside the small intestine through separate transport mechanisms [ ].

Oftentimes, products contain proteins that have been pre-exposed to specific digestive enzymes causing hydrolysis of the proteins into di, tri, and tetrapeptides. A plethora of studies have investigated the effects of the degree of protein fractionation or degree of hydrolysis on the absorption of amino acids and the subsequent hormonal response [ , , , , , ].

Further, the rate of absorption may lead to a more favorable anabolic hormonal environment [ , , ]. Calbet et al. Each of the nitrogen containing solutions contained 15 g of glucose and 30 g of protein.

Results indicated that peptide hydrolysates produced a faster increase in venous plasma amino acids compared to milk proteins. Further, the peptide hydrolysates produced peak plasma insulin levels that were two- and four-times greater than that evoked by the milk and glucose solutions, respectively, with a correlation of 0.

In a more appropriate comparison, Morifuji et al. However, Calbet et al. The hydrolyzed casein, however, did result in a greater amino acid response than the nonhydrolyzed casein. Finally, both hydrolyzed groups resulted in greater gastric secretions, as well as greater plasma increases, in glucose-dependent insulinotropic polypeptides [ ].

Buckley and colleagues [ ] found that a ~ 30 g dose of a hydrolyzed whey protein isolate resulted in a more rapid recovery of muscle force-generating capacity following eccentric exercise, compared with a flavored water placebo or a non-hydrolyzed form of the same whey protein isolate.

In agreement with these findings, Cooke et al. Three and seven days after completing the damaging exercise bout, maximal strength levels were higher in the hydrolyzed whey protein group compared to carbohydrate supplementation.

Additionally, blood concentrations of muscle damage markers tended to be lower when four ~g doses of a hydrolyzed whey protein isolate were ingested for two weeks following the damaging bout. Beyond influencing strength recovery after damaging exercise, other benefits of hydrolyzed proteins have been suggested.

For example, Morifuji et al. Furthermore, Lockwood et al. Results indicated that strength and lean body mass LBM increased equally in all groups.

However, fat mass decreased only in the hydrolyzed whey protein group. While more work needs to be completed to fully determine the potential impact of hydrolyzed proteins on strength and body composition changes, this initial study suggests that hydrolyzed whey may be efficacious for decreasing body fat.

Finally, Saunders et al. The authors reported that co-ingestion of a carbohydrate and protein hydrolysate improved time-trial performance late in the exercise protocol and significantly reduced soreness and markers of muscle damage. Two excellent reviews on the topic of hydrolyzed proteins and their impact on performance and recovery have been published by Van Loon et al.

The prevalence of digestive enzymes in sports nutrition products has increased during recent years with many products now containing a combination of proteases and lipases, with the addition of carbohydrates in plant proteins.

Proteases can hydrolyze proteins into various peptide configurations and potentially single amino acids. It appears that digestive enzyme capabilities and production decrease with age [ ], thus increasing the difficulty with which the body can break down and digest large meals.

Digestive enzymes could potentially work to promote optimal digestion by allowing up-regulation of various metabolic enzymes that may be needed to allow for efficient bodily operation.

Further, digestive enzymes have been shown to minimize quality differences between varying protein sources [ ]. Individuals looking to increase plasma peak amino acid concentrations may benefit from hydrolyzed protein sources or protein supplemented with digestive enzymes.

However, more work is needed before definitive conclusions can be drawn regarding the efficacy of digestive enzymes. Despite a plethora of studies demonstrating safety, much concern still exists surrounding the clinical implications of consuming increased amounts of protein, particularly on renal and hepatic health.

The majority of these concerns stem from renal failure patients and educational dogma that has not been rewritten as evidence mounts to the contrary. Certainly, it is clear that people in renal failure benefit from protein-restricted diets [ ], but extending this pathophysiology to otherwise healthy exercise-trained individuals who are not clinically compromised is inappropriate.

Published reviews on this topic consistently report that an increased intake of protein by competitive athletes and active individuals provides no indication of hepato-renal harm or damage [ , ].

This is supported by a recent commentary [ ] which referenced recent reports from the World Health Organization [ ] where they indicated a lack of evidence linking a high protein diet to renal disease.

Likewise, the panel charged with establishing reference nutrient values for Australia and New Zealand also stated there was no published evidence that elevated intakes of protein exerted any negative impact on kidney function in athletes or in general [ ].

Recently, Antonio and colleagues published a series of original investigations that prescribed extremely high amounts of protein ~3. The first study in had resistance-trained individuals consume an extremely high protein diet 4.

A follow-up investigation [ ] required participants to ingest up to 3. Their next study employed a crossover study design in twelve healthy resistance-trained men in which each participant was tested before and after for body composition as well as blood-markers of health and performance [ ].

In one eight-week block, participants followed their normal habitual diet 2. No changes in body composition were reported, and importantly, no clinical side effects were observed throughout the study. Finally, the same group of authors published a one-year crossover study [ ] in fourteen healthy resistance-trained men.

This investigation showed that the chronic consumption of a high protein diet i. Furthermore, there were no alterations in clinical markers of metabolism and blood lipids.

Multiple review articles indicate that no controlled scientific evidence exists indicating that increased intakes of protein pose any health risks in healthy, exercising individuals.

A series of controlled investigations spanning up to one year in duration utilizing protein intakes of up to 2. In alignment with our previous position stand, it is the position of the International Society of Sports Nutrition that the majority of exercising individuals should consume at minimum approximately 1.

The amount is dependent upon the mode and intensity of the exercise, the quality of the protein ingested, as well as the energy and carbohydrate status of the individual. Concerns that protein intake within this range is unhealthy are unfounded in healthy, exercising individuals.

An attempt should be made to consume whole foods that contain high-quality e. The timing of protein intake in the period encompassing the exercise session may offer several benefits including improved recovery and greater gains in lean body mass.

In addition, consuming protein pre-sleep has been shown to increase overnight MPS and next-morning metabolism acutely along with improvements in muscle size and strength over 12 weeks of resistance training. Intact protein supplements, EAAs and leucine have been shown to be beneficial for the exercising individual by increasing the rates of MPS, decreasing muscle protein degradation, and possibly aiding in recovery from exercise.

In summary, increasing protein intake using whole foods as well as high-quality supplemental protein sources can improve the adaptive response to training. Campbell B, Kreider RB, Ziegenfuss T, La Bounty P, Roberts M, Burke D, et al. International society of sports nutrition position stand: protein and exercise.

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Adding 20—25 grams of protein can further speed up recovery and promote protein production in your muscles 2. SUMMARY Consuming a good amount of carbs and protein immediately after training can help maintain your sports performance during weight loss.

Individuals attempting to lose weight are often at risk of losing some muscle in addition to fat. Athletes are no exception. Some muscle loss can be prevented by eating a sufficient amount of protein, avoiding crash diets, and lifting weights 3.

Research shows that both protein intake and strength-training exercises stimulate muscle protein synthesis. Nevertheless, make sure to speak to your coach before adding any extra workouts to your schedule. This will reduce your risk of overtraining or injuries.

SUMMARY Strength-training exercises can help prevent the muscle loss often experienced during a period of weight loss. Researchers believe these adaptations can persist for some time after you bump up your calorie intake and cause you to quickly regain the lost fat 5.

This may help restore your hormone levels and metabolism better, minimizing the weight regain 5. SUMMARY Increasing your calorie intake gradually after a period of weight loss may help minimize weight regain.

Although weight loss is a widely researched topic, the number of studies performed on athletes is limited. Nevertheless, many of the strategies scientifically proven to help non-athletes lose body fat may also benefit athletes. Thus, you can try some of the following:.

SUMMARY Stress, sleep, hydration, and alcohol all affect weight loss. Eating slowly, controlling portion sizes, and sleeping well can all help you lose weight. Those who want to reduce their body fat levels should aim to do so during the off-season.

Keep in mind that lower body fat is not always better. Athletes should discuss any weight loss goals or strategies with their coach or sports dietitian. Our experts continually monitor the health and wellness space, and we update our articles when new information becomes available.

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How Well Do You Sleep? Health Conditions Discover Plan Connect. The target level of protein intake within this recommended range requires consideration of a number of case-specific factors including the athlete's body composition, habitual protein intake and broader nutrition goals.

Athletes should focus on consuming high-quality protein sources, aiming to consume protein feedings evenly spaced throughout the day. Post-exercise consumption of 0.

From protein powders to athleges breakfast cereals, ayhletes seems losd protein is everywhere these Continuous glucose monitoring for better diabetes management. Weoght, a lot of popular Body fat calipers for professionals diets have been Prrotein waves—the macronutrient is central Prootein both keto and Oral medication for gestational diabetes plans. So, are carbs no BPA-Free Packaging king? In general, protein is a crucial element of good nutrition. One of the three macronutrientsalong with carbohydrates and fat, protein is incredibly important for our health. The amount of protein you should eat depends on a few factors, including age, sex, body size, and activity level. High-protein diets encourage eating more of the macronutrient than what you might be accustomed to, in order to boost weight loss, improve energyand enhance athletic performance. There Olive oil and vinegar a large body of Proteim evidence Body fat calipers for professionals support protein Protein for weight loss in athletes in ahtletes of the atheltes dietary allowance RDA 0. Diet-induced weight loss with as low as possible ratio fpr skeletal muscle to losd mass loss is a situation we refer to as high-quality weight loss. We propose that high-quality weight loss is often of importance to elite athletes in order to maintain their muscle engine and shed unwanted fat mass, potentially improving athletic performance. Current recommendations for protein intakes during weight loss in athletes are set at 1. However, the severity of the caloric deficit and type and intensity of training performed by the athlete will influence at what end of this range athletes choose to be.

Protein for weight loss in athletes -

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Wycherley , T. Effects of energy-restricted high-protein, low-fat compared with standard-protein, low-fat diets: A meta-analysis of randomized controlled trials. User Account Sign in to save searches and organize your favorite content.

Not registered? Sign up My Content 0 Recently viewed 0 Save Entry. Recently viewed 0 Save Search. Human Kinetics. Previous Article Next Article. Protein Recommendations for Weight Loss in Elite Athletes: A Focus on Body Composition and Performance.

in International Journal of Sport Nutrition and Exercise Metabolism. Amy J. Hector Amy J. Hector McMaster University Search for other papers by Amy J.

Hector in Current site Google Scholar PubMed Close. Stuart M. Phillips Stuart M. Phillips McMaster University Search for other papers by Stuart M.

Phillips in Current site Google Scholar PubMed Close. In Print: Volume Issue 2. Page Range: — Open access. Get Citation Alerts. Download PDF. Abstract Full Text PDF Author Notes. Optimal Protein Intake During Caloric Restriction in Elite Athletes: How Much Protein?

Figure 1 —Summary of studies in the systematic review by Helms et al. Optimal Protein Intake During Caloric Restriction in Elite Athletes: Protein Timing and Quality Additional considerations for optimal protein intake during dietary energy restriction include the timing and dose of protein ingestion and the quality of the protein source, which have been reviewed in greater detail elsewhere Murphy et al.

Protein-Derived Supplements to Promote High-Quality Weight Loss Another method to promote high-quality weight loss in a restricted energy budget is the use of dietary supplements. Figure 2 —Figure based on Churchward-Venne et al. Protein for Performance During Dietary Energy Restriction Many athletes may undergo aggressive weight loss protocols particularly in weight-category sports in order to rapidly achieve desired body weight.

Influence of Higher Protein Intakes on Health Common concerns regarding the consumption of high-protein diets are the effects of elevated protein on kidney function and bone health, and the lack of scientific evidence to support these claims has been discussed in more detail in the following review articles Phillips, ; Phillips et al.

Summary There is demonstrable benefit to the consumption of higher than recommended protein intakes, greater than the RDA, for promoting high-quality weight loss and maintaining or improving athletic performance during dietary energy restriction. Figure 3 —Hypothetical illustration of protein requirements to spare lean mass increasing with greater energy deficits.

x Elia , M. x false. PubMed Hartman , J. x Heymsfield , S. PubMed Humayun , M. PubMed false. An important research design note, however, is that those studies which reported improvements in endurance performance when protein was added to a carbohydrate beverage before and during exercise all used a time-to-exhaustion test [ 10 , 11 , 12 ].

When specifically interested in performance outcomes, a time trial is preferred as it better mimics competition and pacing demands. In conclusion, added protein does not appear to improve endurance performance when given for several days, weeks, or immediately prior to and during endurance exercise.

For these reasons, it seems prudent to recommend for endurance athletes to ingest approximately 0. Another important consideration relates to the impact of ingesting protein along with carbohydrate on rates of protein synthesis and balance during prolonged bouts of endurance exercise.

Beelen and colleagues [ 14 ] determined that adding protein to carbohydrate consumption throughout a prolonged bout of endurance exercise promotes a higher whole body net protein balance, but the added protein does not exert any further impact on rates of MPS. While performance outcomes were not measured, these results shift the focus of nutrient ingestion during prolonged bouts of endurance exercise to the ingestion of carbohydrate.

When adequate carbohydrate is delivered, adding protein to carbohydrate does not appear to improve endurance performance over the course of a few days or weeks. Adding protein during or after an intensive bout of endurance exercise may suppress the rise in plasma proteins linked to myofibrillar damage and reduce feelings of muscle soreness.

There are relatively few investigations on the effects of protein supplementation on endurance performance. The extent to which protein supplementation, in conjunction with resistance training, enhances maximal strength is contingent upon many factors, including:.

Co-ingestion of additional dietary ingredients that may favorably impact strength e. creatine, HMB. Taking each of these variables into consideration, the effects of supplemental protein consumption has on maximal strength enhancement are varied, with a majority of the investigations reporting no benefit [ 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 ] and a few reporting improvements in maximal strength [ 26 , 27 , 28 , 29 ].

With limited exceptions [ 16 , 18 , 23 , 27 ], most of the studies utilized young, healthy, untrained males as participants. In one investigation examining college football athletes supplementing with a proprietary milk protein supplement two servings of 42 g per day for 12 weeks, a These differences were statistically significant.

When females were the only sex investigated, the outcomes consistently indicated that supplemental protein does not appear to enhance maximal strength at magnitudes that reach statistical significance. Hida et al. An important note for this study is that 15 g of egg protein is considered by many to be a sub-optimal dose [ 31 ].

However, others have advocated that the total daily intake of protein might be as important or more important [ 32 ]. In another study, Josse et al. In summary, while research investigating the addition of supplemental protein to a diet with adequate energy and nutrient intakes is inconclusive in regards to stimulating strength gains in conjunction with a resistance-training program to a statistically significant degree, greater protein intakes that are achieved from both dietary and supplemental sources do appear to have some advantage.

Hoffman and colleagues [ 29 ] reported that in athletes consuming daily protein intakes above 2. Cermak and colleagues [ 35 ] pooled the outcomes from 22 separate clinical trials to yield subjects in their statistical analysis and found that protein supplementation with resistance training resulted in a A similar conclusion was also drawn by Pasiakos et al.

Results from many single investigations indicate that in both men and women protein supplementation exerts a small to modest impact on strength development. Pooled results of multiple studies using meta-analytic and other systematic approaches consistently indicate that protein supplementation 15 to 25 g over 4 to 21 weeks exerts a positive impact on performance.

Andersen et al. When the blend of milk proteins was provided, significantly greater increases in fat-free mass, muscle cross-sectional area in both the Type I and Type II muscle fibers occurred when compared to changes seen with carbohydrate consumption.

Collectively, a meta-analysis by Cermak and colleagues [ 35 ] reported a mean increase in fat-free mass of 0. Other reviews by Tipton, Phillips and Pasiakos, respectively, [ 36 , 38 , 39 ] provide further support that protein supplementation 15—25 g over 4—14 weeks augments lean mass accretion when combined with completion of a resistance training program.

Beyond accretion of fat-free mass, increasing daily protein intake through a combination of food and supplementation to levels above the recommended daily allowance RDA RDA 0. The majority of this work has been conducted using overweight and obese individuals who were prescribed an energy-restricted diet that delivered a greater ratio of protein relative to carbohydrate.

Greater amounts of fat were lost when higher amounts of protein were ingested, but even greater amounts of fat loss occurred when the exercise program was added to the high-protein diet group, resulting in significant decreases in body fat.

Each person was randomly assigned to consume a diet that contained either 1× 0. Participants were measured for changes in body weight and body composition. While the greatest body weight loss occurred in the 1× RDA group, this group also lost the highest percentage of fat-free mass and lowest percentage of fat mass.

Collectively, these results indicate that increasing dietary protein can promote favorable adaptations in body composition through the promotion of fat-free mass accretion when combined with a hyperenergetic diet and a heavy resistance training program and can also promote the loss of fat mass when higher intakes of daily protein × the RDA are combined with an exercise program and a hypoenergetic diet.

When combined with a hyperenergetic diet and a heavy resistance-training program, protein supplementation may promote increases in skeletal muscle cross-sectional area and lean body mass. When combined with a resistance-training program and a hypoenergetic diet, an elevated daily intake of protein 2 — 3× the RDA can promote greater losses of fat mass and greater overall improvements in body composition.

In the absence of feeding, muscle protein balance remains negative in response to an acute bout of resistance exercise [ 48 ]. Tipton et al. Later, Burd et al. Subsequently, these conclusions were supported by Borsheim [ 52 ] and Volpi [ 53 ].

The study by Borsheim also documented a dose-response outcome characterized by a near doubling of net protein balance in response to a three to six gram dose of the EAAs [ 52 ].

Building on this work, Tipton et al. These findings formed the theoretical concept of protein timing for resistance exercise that has since been transferred to not only other short-duration, high-intensity activities [ 56 ] but also endurance-based sports [ 57 ] and subsequent performance outcomes [ 58 ].

The strategic consumption of nutrition, namely protein or various forms of amino acids, in the hours immediately before and during exercise i.

While earlier investigations reported positive effects from consumption of amino acids [ 37 , 46 , 61 ], it is now clear that intact protein supplements such as egg, whey, casein, beef, soy and even whole milk can evoke an anabolic response that can be similar or greater in magnitude to free form amino acids, assuming ingestion of equal EAA amounts [ 62 , 63 , 64 ].

For instance, whey protein ingested close to resistance exercise, promotes a higher activation phosphorylation of mTOR a key signaling protein found in myocytes that is linked to the synthesis of muscle proteins and its downstream mRNA translational signaling proteins i.

Moreover, it was found that the increased mTOR signaling corresponded with significantly greater muscle hypertrophy after 10 weeks of training [ 65 ]. However, the hypertrophic differences between protein consumption and a non-caloric placebo appeared to plateau by week 21, despite a persistently greater activation of this molecular signaling pathway from supplementation.

Results from other research groups [ 56 , 57 , 58 , 66 ] show that timing of protein near ± 2 h aerobic and anaerobic exercise training appears to provide a greater activation of the molecular signalling pathways that regulate myofibrillar and mitochondrial protein synthesis as well as glycogen synthesis.

It is widely reported that protein consumption directly after resistance exercise is an effective way to acutely promote a positive muscle protein balance [ 31 , 55 , 67 ], which if repeated over time should translate into a net gain or hypertrophy of muscle [ 68 ]. Pennings and colleagues [ 69 ] reported an increase in both the delivery and incorporation of dietary proteins into the skeletal muscle of young and older adults when protein was ingested shortly after completion of exercise.

These findings and others add to the theoretical basis for consumption of post-protein sooner rather than later after exercise, since post workout MPS rates peak within three hours and remain elevated for an additional 24—72 h [ 50 , 70 ].

This extended time frame also provides a rationale for both immediate and sustained i. These temporal considerations would also capture the peak elevation in signalling proteins shown to be pivotal for increasing the initiation of translation of muscle proteins, which for the most part appears to peak between 30 and 60 min after exercise [ 71 ].

However, these differences may be related to the type of protein used between the studies. The studies showing positive effects of protein timing used milk proteins, whereas the latter study used a collagen based protein supplement.

While a great deal of work has focused on post-exercise protein ingestion, other studies have suggested that pre-exercise and even intra-exercise ingestion may also support favorable changes in MPS and muscle protein breakdown [ 14 , 54 , 75 , 76 , 77 , 78 ].

Initially, Tipton and colleagues [ 54 ] directly compared immediate pre-exercise and immediate post-exercise ingestion of a mixture of carbohydrate 35 g and EAAs 6 g combination on changes in MPS. They reported that pre-exercise ingestion promoted higher rates of MPS while also demonstrating that nutrient ingestion prior to exercise increased nutrient delivery to a much greater extent than other immediate or one hour post-exercise time points.

These results were later challenged by Fujita in who employed an identical study design with a different tracer incorporation approach and concluded there was no difference between pre- or post-exercise ingestion [ 75 ].

Subsequent work by Tipton [ 79 ] also found that similar elevated rates of MPS were achieved when ingesting 20 g of a whey protein isolate immediately before or immediately after resistance exercise.

At this point, whether any particular time of protein ingestion confers any unique advantage over other time points throughout a h day to improve strength and hypertrophy has yet to be adequately investigated.

To date, although a substantial amount of literature discusses this concept [ 60 , 80 ], a limited number of training studies have assessed whether immediate pre- and post-exercise protein consumption provides unique advantages compared to other time points [ 72 , 73 , 81 ].

Each study differed in population, training program, environment and nutrition utilized, with each reporting a different result. What is becoming clear is that the subject population, nutrition habits, dosing protocols on both training and non-training days, energy and macronutrient intake, as well as the exercise bout or training program itself should be carefully considered alongside the results.

In particular, the daily amount of protein intake seems to operate as a key consideration because the benefits of protein timing in relation to the peri-workout period seem to be lessened for people who are already ingesting appropriate amounts of protein e.

A literature review by Aragon and Schoenfeld [ 83 ] determined that while compelling evidence exists showing muscle is sensitized to protein ingestion following training, the increased sensitivity to protein ingestion might be greatest in the first five to six hours following exercise.

Thus, the importance of timing may be largely dependent on when a pre-workout meal was consumed, the size and composition of that meal and the total daily protein in the diet.

In this respect, a pre-exercise meal will provide amino acids during and after exercise and therefore it stands to reason there is less need for immediate post-exercise protein ingestion if a pre-exercise meal is consumed less than five hours before the anticipated completion of a workout.

A meta-analysis by Schoenfeld et al. The authors concluded that total protein intake was the strongest predictor of muscular hypertrophy and that protein timing likely influences hypertrophy to a lesser degree. However, the conclusions from this meta-analysis may be questioned because the majority of the studies analyzed were not protein timing studies but rather protein supplementation studies.

In that respect, the meta-analysis provides evidence that protein supplementation i. While a strong rationale remains to support the concept that the hours immediately before or after resistance exercise represents an opportune time to deliver key nutrients that will drive the accretion of fat-free mass and possibly other favorable adaptations, the majority of available literature suggests that other factors may indeed be operating to a similar degree that ultimately impact the observed adaptations.

In this respect, a key variable that must be accounted for is the absolute need for energy and protein required to appropriately set the body up to accumulate fat-free mass.

Thus, the most practical recommendation is to have athletes consume a meal during the post-workout or pre-workout time period since it may either help or have a neutral effect. In younger subjects, the ingestion of 20—30 g of any high biological value protein before or after resistance exercise appears to be sufficient to maximally stimulate MPS [ 21 , 64 ].

More recently, Macnaughton and colleagues [ 85 ] reported that 40 g of whey protein ingestion significantly increased the MPS responses compared to a 20 g feeding after an acute bout of whole-body resistance exercise, and that the absolute protein dose may operate as a more important consideration than providing a protein dose that is normalized to lean mass.

Free form EAAs, soy, milk, whey, caseinate, and other protein hydrolysates are all capable of activating MPS [ 86 ]. However, maximal stimulation of MPS, which results in higher net muscle protein accretion, is the product of the total amount of EAA in circulation as well as the pattern and appearance rate of aminoacidemia that modulates the MPS response [ 86 ].

Recent work has clarified that whey protein provides a distinct advantage over other protein sources including soy considered another fast absorbing protein and casein a slower acting protein source on acute stimulation of MPS [ 86 , 87 ].

Importantly, an elegant study by West and investigators [ 87 ] sought to match the delivery of EAAs in feeding patterns that replicated how whey and casein are digested.

The authors reported that a 25 g dose of whey protein that promoted rapid aminoacidemia further enhanced MPS and anabolic signaling when compared to an identical total dose of whey protein when delivered as ten separate 2.

The advantages of whey protein are important to consider, particularly as all three sources rank similarly in assessments of protein quality [ 88 ].

In addition to soy, other plant sources e. have garnered interest as potential protein sources to consider. Unfortunately, research that examines the ability of these protein sources to modulate exercise performance and training adaptations is limited at this time.

The investigators concluded that gains in strength, muscle thickness and body composition were similar between the two protein groups, suggesting that rice protein may be a suitable alternative to whey protein at promoting resistance training adaptations.

Furthermore, differences in absorption kinetics, and the subsequent impact on muscle protein metabolism appear to extend beyond the degree of hydrolysis and amino acid profiles [ 69 , 86 , 90 , 91 , 92 , 92 ]. For instance, unlike soy more of the EAAs from whey proteins hydrolysates and isolates survive splanchnic uptake and travel to the periphery to activate a higher net gain in muscle [ 86 ].

These characteristics yield a high concentration of amino acids in the blood aminoacidemia [ 69 , 87 ] that facilitates greater activation of MPS and net muscle protein accretion, in direct comparison to other protein choices [ 50 , 69 , 91 ].

The addition of creatine to whey protein supplementation appears to further augment these adaptations [ 27 , 72 , 95 ]; however, an optimal timing strategy for this combination remains unclear.

The timing of protein-rich meals consumed throughout a day has the potential to influence adaptations to exercise. Using similar methods, other studies over recent decades [ 53 , 62 , 87 , 91 , 96 , 97 , 98 , 99 , ] have established the following:.

The anabolic response to feeding is pronounced but transient. During the post-prandial phase 1—4 h after a meal MPS is elevated, resulting in a positive muscle protein balance.

In contrast, MPS rates are lower in a fasted state and muscle protein balance is negative. Protein accretion only occurs in the fed state. The concentration of EAA in the blood plasma regulates protein synthesis rates within muscle at rest and post exercise.

More recent work has established that protein-carbohydrate supplementation after strenuous endurance exercise stimulates contractile MPS via similar signaling pathways as resistance exercise [ 56 , 57 ]. That is, the consumption of a protein-containing meal up to 24 h after a single bout of resistance exercise results in a higher net stimulation of MPS and protein accretion than the same meal consumed after 24 h of inactivity [ 50 ].

The effect of insulin on MPS is dependent on its ability to increase amino acid availability, which does not occur when insulin is systematically increased e. Taken together, these results seem to indicate that post-workout carbohydrate supplementation offers very little contribution from a muscle development standpoint provided adequate protein is consumed.

Importantly, these results are not to be interpreted to mean that carbohydrate administration offers no potential effect for an athlete engaging in moderate to high volumes of training, but rather that benefits derived from carbohydrate administration appear to more favorably impact aspects of muscle glycogen recovery as opposed to stimulating muscle protein accretion.

Eating before sleep has long been controversial [ , , ]. However, a methodological consideration in the original studies such as the population used, time of feeding, and size of the pre-sleep meal confounds firm conclusions about benefits or drawbacks.

Results from several investigations indicate that 30—40 g of casein protein ingested min prior to sleep [ ] or via nasogastric tubing [ ] increased overnight MPS in both young and old men, respectively.

Likewise, in an acute setting, 30 g of whey protein, 30 g of casein protein, and 33 g of carbohydrate consumed min prior to sleep resulted in an elevated morning resting metabolic rate in young fit men compared to a non-caloric placebo [ ].

Interestingly, Madzima et al. This infers that casein protein consumed pre-sleep maintains overnight lipolysis and fat oxidation. This finding was further supported by Kinsey et al. Similar to Madzima et al. Interestingly, the pre-sleep protein and carbohydrate ingestion resulted in elevated insulin concentrations the next morning and decreased hunger in this overweight population.

Of note, it appears that exercise training completely ameliorates any rise in insulin when eating at night before sleep [ ], while the combination of pre-sleep protein and exercise has been shown to reduce blood pressure and arterial stiffness in young obese women with prehypertension and hypertension [ ].

In athletes, evening chocolate milk consumption has also been shown to influence carbohydrate metabolism in the morning, but not running performance [ ]. In addition, data supports that exercise performed in the evening augments the overnight MPS response in both younger and older men [ , , ].

To date, only a few studies involving nighttime protein ingestion have been carried out for longer than four weeks. Snijders et al. The group receiving the protein-centric supplement each night before sleep had greater improvements in muscle mass and strength over the week study.

Of note, this study was non-nitrogen balanced and the protein group received approximately 1. More recently, in a study in which total protein intake was equal, Antonio et al. They examined the effects on body composition and performance [ ]. All subjects maintained their usual exercise program. The authors reported no differences in body composition or performance between the morning and evening casein supplementation groups.

However, it is worth noting that, although not statistically significant, the morning group added 0. Although this finding was not statistically significant, it supports data from Burk et al. It should be noted that the subjects in the Burk et al. study were resistance training.

A retrospective epidemiological study by Buckner et al. Thus, it appears that protein consumption in the evening before sleep might be an underutilized time to take advantage of a protein feeding opportunity that can potentially improve body composition and performance. In addition to direct assessments of timed administration of nutrients, other studies have explored questions that center upon the pattern of when certain protein-containing meals are consumed.

Paddon-Jones et al. In this study, participants were given an EAA supplement three times a day for 28 days. Results indicated that acute stimulation of MPS provided by the supplement on day 1 resulted in a net gain of ~7.

When extrapolated over the entire day study, the predicted change in muscle mass corresponded to the actual change in muscle mass ~ g measured by dual-energy x-ray absorptiometry DEXA [ 97 ].

While these findings are important, it is vital to highlight that this study incorporated a bed rest model with no acute exercise stimulus while other work by Mitchell et al. Interestingly, supplementation with 15 g of EAAs and 30 g of carbohydrate produced a greater anabolic effect increase in net phenylalanine balance than the ingestion of a mixed macronutrient meal, despite the fact that both interventions contained a similar dose of EAAs [ 96 ].

Most importantly, the consumption of the supplement did not interfere with the normal anabolic response to the meal consumed three hours later [ 96 ].

Areta et al. The researchers compared the anabolic responses of three different patterns of ingestion a total of 80 g of protein throughout a h recovery period after resistance exercise. Using a group of healthy young adult males, the protein feeding strategies consisted of small pulsed 8 × 10 g , intermediate 4 × 20 g , or bolus 2 × 40 g administration of whey protein over the h measurement window.

Results showed that the intermediate dosing 4 × 20 g was superior for stimulating MPS for the h experimental period. Specifically, the rates of myofibrillar protein synthesis were optimized throughout the day of recovery by the consumption of 20 g protein every three hours compared to large 2 × 40 g , less frequent servings or smaller but more frequent 8 × 10 g patterns of protein intake [ 67 ].

Previously, the effect of various protein feeding strategies on skeletal MPS during an entire day was unknown. This study provided novel information demonstrating that the regulation of MPS can be modulated by the timing and distribution of protein over 12 h after a single bout of resistance exercise.

However, it should be noted that an 80 g dose of protein over a h period is quite low. The logical next step for researchers is to extend these findings into longitudinal training studies to see if these patterns can significantly affect resistance-training adaptations.

Indeed, published studies by Arnal [ ] and Tinsley [ ] have all made some attempt to examine the impact of adjusting the pattern of protein consumption across the day in combination with various forms of exercise. Collective results from these studies are mixed.

Thus, future studies in young adults should be designed to compare a balanced vs. skewed distribution pattern of daily protein intake on the daytime stimulation of MPS under resting and post-exercise conditions and training-induced changes in muscle mass, while taking into consideration the established optimal dose of protein contained in a single serving for young adults.

Without more conclusive evidence spanning several weeks, it seems pragmatic to recommend the consumption of at least g of protein ~0. In the absence of feeding and in response to resistance exercise, muscle protein balance remains negative.

Skeletal muscle is sensitized to the effects of protein and amino acids for up to 24 h after completion of a bout of resistance exercise. A protein dose of 20—40 g of protein 10—12 g of EAAs, 1—3 g of leucine stimulates MPS, which can help to promote a positive nitrogen balance.

The EAAs are critically needed for achieving maximal rates of MPS making high-quality, protein sources that are rich in EAAs and leucine the preferred sources of protein.

Studies have suggested that pre-exercise feedings of amino acids in combination with carbohydrate can achieve maximal rates of MPS, but protein and amino acid feedings during this time are not clearly documented to increase exercise performance.

Total protein and calorie intake appears to be the most important consideration when it comes to promoting positive adaptations to resistance training, and the impact of timing strategies immediately before or immediately after to heighten these adaptations in non-athletic populations appears to be minimal.

Proteins provide the building blocks of all tissues via their constituent amino acids. Athletes consume dietary protein to repair and rebuild skeletal muscle and connective tissues following intense training bouts or athletic events. A report in by Phillips [ ] summarized the findings surrounding protein requirements in resistance-trained athletes.

Using a regression approach, he concluded that a protein intake of 1. A key consideration regarding these recommended values is that all generated data were obtained using the nitrogen balance technique, which is known to underestimate protein requirements.

Interestingly, two of the included papers had prescribed protein intakes of 2. All data points from these two studies also had the highest levels of positive nitrogen balance. For an athlete seeking to ensure an anabolic environment, higher daily protein intakes might be needed.

Another challenge that underpins the ability to universally and successfully recommend daily protein amounts are factors related to the volume of the exercise program, age, body composition and training status of the athlete; as well as the total energy intake in the diet, particularly for athletes who desire to lose fat and are restricting calories to accomplish this goal [ ].

For these reasons, and due to an increase of published studies in areas related to optimal protein dosing, timing and composition, protein needs are being recommended within this position stand on a per meal basis.

For example, Moore [ 31 ] found that muscle and albumin protein synthesis was optimized at approximately 20 g of egg protein at rest. Witard et al. Furthermore, while results from these studies offer indications of what optimal absolute dosing amounts may be, Phillips [ ] concluded that a relative dose of 0.

Once a total daily target protein intake has been achieved, the frequency and pattern with which optimal doses are ingested may serve as a key determinant of overall changes in protein synthetic rates. Research indicates that rates of MPS rapidly rise to peak levels within 30 min of protein ingestion and are maintained for up to three hours before rapidly beginning to lower to basal rates of MPS even though amino acids are still elevated in the blood [ ].

Using an oral ingestion model of 48 g of whey protein in healthy young men, rates of myofibrillar protein synthesis increased three-fold within 45—90 min before slowly declining to basal rates of MPS all while plasma concentration of EAAs remained significantly elevated [ ].

While largely unexplored in a human model, these authors relied upon an animal model and were able to reinstate increases in MPS using the consumption of leucine and carbohydrate min after ingestion of the first meal. As such, it is suggested that individuals attempting to restrict caloric intake should consume three to four whole meals consisting of 20—40 g of protein per meal.

While this recommendation stems primarily from initial work that indicated protein doses of 20—40 g favorably promote increased rates of MPS [ 31 , , ], Kim and colleagues [ ] recently reported that a 70 g dose of protein promoted a more favorable net balance of protein when compared to a 40 g dose due to a stronger attenuation of rates of muscle protein breakdown.

For those attempting to increase their calories, we suggest consuming small snacks between meals consisting of both a complete protein and a carbohydrate source. This contention is supported by research from Paddon-Jones et al.

These researchers compared three cal mixed macronutrient meals to three cal meals combined with three cal amino acid-carbohydrate snacks between meals. Additionally, using a protein distribution pattern of 20—25 g doses every three hours in response to a single bout of lower body resistance exercise appears to promote the greatest increase in MPS rates and phosphorylation of key intramuscular proteins linked to muscle hypertrophy [ ].

This simple addition could provide benefits for individuals looking to increase muscle mass and improve body composition in general while also striving to maintain or improve health and performance.

The current RDA for protein is 0. While previous recommendations have suggested a daily intake of 1.

Daily and per dose needs are combinations of many factors including volume of exercise, age, body composition, total energy intake and training status of the athlete.

Daily intakes of 1. Even higher amounts ~70 g appear to be necessary to promote attenuation of muscle protein breakdown. Pacing or spreading these feeding episodes approximately three hours apart has been consistently reported to promote sustained, increased levels of MPS and performance benefits.

There are 20 total amino acids, comprised of 9 EAAs and 11 non-essential amino acids NEAAs. EAAs cannot be produced in the body and therefore must be consumed in the diet.

Several methods exist to determine protein quality such as Chemical Score, Protein Efficiency Ratio, Biological Value, Protein Digestibility-Corrected Amino Acid Score PDCAAS and most recently, the Indicator Amino Acid Oxidation IAAO technique.

Ultimately, in vivo protein quality is typically defined as how effective a protein is at stimulating MPS and promoting muscle hypertrophy [ ]. Overall, research has shown that products containing animal and dairy-based proteins contain the highest percentage of EAAs and result in greater hypertrophy and protein synthesis following resistance training when compared to a vegetarian protein-matched control, which typically lacks one or more EAAs [ 86 , 93 , ].

Several studies, but not all, [ ] have indicated that EAAs alone stimulate protein synthesis in the same magnitude as a whole protein with the same EAA content [ 98 ]. For example, Borsheim et al. Moreover, Paddon-Jones and colleagues [ 96 ] found that a cal supplement containing 15 g of EAAs stimulated greater rates of protein synthesis than an cal meal with the same EAA content from a whole protein source.

While important, the impact of a larger meal on changes in circulation and the subsequent delivery of the relevant amino acids to the muscle might operate as important considerations when interpreting this data.

In contrast, Katsanos and colleagues [ ] had 15 elderly subjects consume either 15 g of whey protein or individual doses of the essential and nonessential amino acids that were identical to what is found in a g whey protein dose on separate occasions.

Whey protein ingestion significantly increased leg phenylalanine balance, an index of muscle protein accrual, while EAA and NEAA ingestion exerted no significant impact on leg phenylalanine balance.

This study, and the results reported by others [ ] have led to the suggestion that an approximate 10 g dose of EAAs might serve as an optimal dose to maximally stimulate MPS and that intact protein feedings of appropriate amounts as opposed to free amino acids to elderly individuals may stimulate greater improvements in leg muscle protein accrual.

Based on this research, scientists have also attempted to determine which of the EAAs are primarily responsible for modulating protein balance. The three branched-chain amino acids BCAAs , leucine, isoleucine, and valine are unique among the EAAs for their roles in protein metabolism [ ], neural function [ , , ], and blood glucose and insulin regulation [ ].

Additionally, enzymes responsible for the degradation of BCAAs operate in a rate-limiting fashion and are found in low levels in splanchnic tissues [ ]. Thus, orally ingested BCAAs appear rapidly in the bloodstream and expose muscle to high concentrations ultimately making them key components of skeletal MPS [ ].

Furthermore, Wilson and colleagues [ ] have recently demonstrated, in an animal model, that leucine ingestion alone and with carbohydrate consumed between meals min post-consumption extends protein synthesis by increasing the energy status of the muscle fiber.

Multiple human studies have supported the contention that leucine drives protein synthesis [ , ]. Moreover, this response may occur in a dose-dependent fashion, plateauing at approximately two g at rest [ 31 , ], and increasing up to 3.

However, it is important to realize that the duration of protein synthesis after resistance exercise appears to be limited by both the signal leucine concentrations , ATP status, as well as the availability of substrate i. As such, increasing leucine concentration may stimulate increases in muscle protein, but a higher total dose of all EAAs as free form amino acids or intact protein sources seems to be most suited for sustaining the increased rates of MPS [ ].

It is well known that exercise improves net muscle protein balance and in the absence of protein feeding, this balance becomes more negative. When combined with protein feeding, net muscle protein balance after exercise becomes positive [ ].

Norton and Layman [ ] proposed that consumption of leucine, could turn a negative protein balance to a positive balance following an intense exercise bout by prolonging the MPS response to feeding.

In support, the ingestion of a protein or essential amino acid complex that contains sufficient amounts of leucine has been shown to shift protein balance to a net positive state after intense exercise training [ 46 , ]. Even though leucine has been demonstrated to independently stimulate protein synthesis, it is important to recognize that supplementation should not be with just leucine alone.

For instance, Wilson et al. In summary, athletes should focus on consuming adequate leucine content in each of their meals through selection of high-quality protein sources [ ]. Protein sources containing higher levels of the EAAs are considered to be higher quality sources of protein.

The body uses 20 amino acids to make proteins, seven of which are essential nine conditionally , requiring their ingestion to meet daily needs.

EAAs appear to be uniquely responsible for increasing MPS with doses ranging from 6 to 15 g all exerting stimulatory effects. In addition, doses of approximately one to three g of leucine per meal appear to be needed to stimulate protein translation machinery.

The BCAAs i. However, the extent to which these changes are aligned with changes in MPS remains to be fully explored. While greater doses of leucine have been shown to independently stimulate increases in protein synthesis, a balanced consumption of the EAAs promotes the greatest increases.

Milk proteins have undergone extensive research related to their potential roles in augmenting adaptations from exercise training [ 86 , 93 ]. For example, consuming milk following exercise has been demonstrated to accelerate recovery from muscle damaging exercise [ ], increase glycogen replenishment [ ], improve hydration status [ , ], and improve protein balance to favor synthesis [ 86 , 93 ], ultimately resulting in increased gains in both neuromuscular strength and skeletal muscle hypertrophy [ 93 ].

Moreover, milk protein contains the highest score on the PDCAAS rating system, and in general contains the greatest density of leucine [ ].

Milk can be fractionated into two protein classes, casein and whey. While both are high in quality, the two differ in the rate at which they digest as well as the impact they have on protein metabolism [ , , ].

Whey protein is water soluble, mixes easily, and is rapidly digested [ ]. In contrast, casein is water insoluble, coagulates in the gut and is digested more slowly than whey protein [ ].

Casein also has intrinsic properties such as opioid peptides, which effectively slow gastric motility [ ]. Original research investigating the effects of digestion rate was conducted by Boirie, Dangin and colleagues [ , , ].

These researchers gave a 30 g bolus of whey protein and a 43 g bolus of casein protein to subjects on separate occasions and measured amino acid levels for several hours after ingestion. They reported that the whey protein condition displayed robust hyperaminoacidemia min after administration.

However, by min, amino acid concentrations had returned to baseline. In contrast, the casein condition resulted in a slow increase in amino acid concentrations, which remained elevated above baseline after min.

Over the study duration, casein produced a greater whole body leucine balance than the whey protein condition, leading the researcher to suggest that prolonged, moderate hyperaminoacidemia is more effective at stimulating increases in whole body protein anabolism than a robust, short lasting hyperaminoacidemia.

While this research appears to support the efficacy of slower digesting proteins, subsequent work has questioned its validity in athletes. The first major criticism is that Boire and colleagues investigated whole body non-muscle and muscle protein balance instead of skeletal myofibrillar MPS.

These findings suggest that changes in whole body protein turnover may poorly reflect the level of skeletal muscle protein metabolism that may be taking place. Trommelen and investigators [ ] examined 24 young men ingesting 30 g of casein protein with or without completion of a single bout of resistance exercise, and concluded that rates of MPS were increased, but whole-body protein synthesis rates were not impacted.

More recently, Tang and colleagues [ 86 ] investigated the effects of administering 22 g of hydrolyzed whey isolate and micellar casein 10 g of EAAs at both rest and following a single bout of resistance training in young males.

Moreover, these researchers reported that whey protein ingestion stimulated greater MPS at both rest and following exercise when compared to casein. In comparison to the control group, both whey and casein significantly increased leucine balance, but no differences were found between the two protein sources for amino acid uptake and muscle protein balance.

Additional research has also demonstrated that 10 weeks of whey protein supplementation in trained bodybuilders resulted in greater gains in lean mass 5. These findings suggest that the faster-digesting whey proteins may be more beneficial for skeletal muscle adaptations than the slower digesting casein.

Skeletal muscle glycogen stores are a critical element to both prolonged and high-intensity exercise. In skeletal muscle, glycogen synthase activity is considered one of the key regulatory factors for glycogen synthesis.

Research has demonstrated that the addition of protein in the form of milk and whey protein isolate 0. Further, the addition of protein facilitates repair and recovery of the exercised muscle [ 12 ].

These effects are thought to be related to a greater insulin response following the exercise bout. Intriguingly, it has also been demonstrated that whey protein enhances glycogen synthesis in the liver and skeletal muscle more than casein in an insulin-independent fashion that appears to be due to its capacity to upregulate glycogen synthase activity [ ].

Therefore, the addition of milk protein to a post-workout meal may augment recovery, improve protein balance, and speed glycogen replenishment. While athletes tend to view whey as the ideal protein for skeletal muscle repair and function it also has several health benefits. In particular, whey protein contains an array of biologically active peptides whose amino acids sequences give them specific signaling effects when liberated in the gut.

Furthermore, whey protein appears to play a role in enhancing lymphatic and immune system responses [ ]. In addition, α-lactalbumin contains an ample supply of tryptophan which increases cognitive performance under stress [ ], improves the quality of sleep [ , ], and may also speed wound healing [ ], properties which could be vital for recovery from combat and contact sporting events.

In addition, lactoferrin is also found in both milk and in whey protein, and has been demonstrated to have antibacterial, antiviral, and antioxidant properties [ ]. Moreover, there is some evidence that whey protein can bind iron and therefore increase its absorption and retention [ ].

Egg protein is often thought of as an ideal protein because its amino acid profile has been used as the standard for comparing other dietary proteins [ ].

Due to their excellent digestibility and amino acid content, eggs are an excellent source of protein for athletes. While the consumption of eggs has been criticized due to their cholesterol content, a growing body of evidence demonstrates the lack of a relationship between egg consumption and coronary heart disease, making egg-based products more appealing [ ].

One large egg has 75 kcal and 6 g of protein, but only 1. Research using eggs as the protein source for athletic performance and body composition is lacking, perhaps due to less funding opportunities relative to funding for dairy. Egg protein may be particularly important for athletes, as this protein source has been demonstrated to significantly increase protein synthesis of both skeletal muscle and plasma proteins after resistance exercise at both 20 and 40 g doses.

Leucine oxidation rates were found to increase following the 40 g dose, suggesting that this amount exceeds an optimal dose [ 31 ]. In addition to providing a cost effective, high-quality source of protein rich in leucine 0.

Functional foods are defined as foods that, by the presence of physiologically active components, provide a health benefit beyond basic nutrition [ ].

According to the Academy of Nutrition and Dietetics, functional foods should be consumed as part of a varied diet on a regular basis, at effective levels [ ]. Thus, it is essential that athletes select foods that meet protein requirements and also optimize health and prevent decrements in immune function following intense training.

Eggs are also rich in choline, a nutrient which may have positive effects on cognitive function [ ]. Moreover, eggs provide an excellent source of the carotenoid-based antioxidants lutein and zeaxanthin [ ]. Also, eggs can be prepared with most meal choices, whether at breakfast, lunch, or dinner.

Such positive properties increase the probability of the athletes adhering to a diet rich in egg protein. Meat proteins are a major staple in the American diet and, depending on the cut of meat, contain varying amounts of fat and cholesterol. Meat proteins are well known to be rich sources of the EAAs [ ].

Beef is a common source of dietary protein and is considered to be of high biological value because it contains the full balance of EAAs in a fraction similar to that found in human skeletal muscle [ ].

A standard serving of Moreover, this 30 g dose of beef protein has been shown to stimulate protein synthesis in both young and elderly subjects [ ]. In addition to its rich content of amino acids, beef and other flesh proteins can serve as important sources of micronutrients such as iron, selenium, vitamins A, B12 and folic acid.

This is a particularly important consideration for pregnant and breastfeeding women. Ultimately, as an essential part of a mixed diet, meat helps to ensure adequate distribution of essential micronutrients and amino acids to the body. Research has shown that significant differences in skeletal muscle mass and body composition between older men who resistance train and either consume meat-based or lactoovovegetarian diet [ ].

Over a week period, whole-body density, fat-free mass, and whole-body muscle mass as measured by urinary creatinine excretion increased in the meat-sourced diet group but decreased in the lactoovovegetarian diet group.

These results indicate that not only do meat-based diets increase fat-free mass, but also they may specifically increase muscle mass, thus supporting the many benefits of meat-based diets.

A diet high in meat protein in older adults may provide an important resource in reducing the risk of sarcopenia. Positive results have also been seen in elite athletes that consume meat-based proteins, as opposed to vegetarian diets [ ].

For example, carnitine is a molecule that transports long-chain fatty acids into mitochondria for oxidation and is found in high amounts in meat. While evidence is lacking to support an increase in fat oxidation with increased carnitine availability, carnitine has been linked to the sparing of muscle glycogen, and decreases in exercise-induced muscle damage [ ].

Certainly, more research is needed to support these assertions. Creatine is a naturally occurring compound found mainly in muscle. Vegetarians have lower total body creatine stores than omnivores, which demonstrates that regular meat eating has a significant effect on human creatine status [ ].

Moreover, creatine supplementation studies with vegetarians indicate that increased creatine uptake levels do exist in people who practice various forms of vegetarianism [ ]. Sharp and investigators [ ] published the only study known to compare different supplemental powdered forms of animal proteins on adaptations to resistance training such as increases in strength and improvements in body composition.

Forty-one men and women performed a standardized resistance-training program over eight weeks and consumed a daily 46 g dose of either hydrolyzed chicken protein, beef protein isolate, or whey protein concentrate in comparison to a control group. All groups experienced similar increases in upper and lower-body strength, but all protein-supplemented groups reported significant increases in lean mass and decreases in fat mass.

Meat-based diets have been shown to include additional overall health benefits. Some studies have found that meat, as a protein source, is associated with higher serum levels of IGF-1 [ ], which in turn is related to increased bone mineralization and fewer fractures [ ].

A highly debated topic in nutrition and epidemiology is whether vegetarian diets are a healthier choice than omnivorous diets. One key difference is the fact that vegetarian diets often lack equivalent amounts of protein when compared to omnivorous diets [ ].

However, with proper supplementation and careful nutritional choices, it is possible to have complete proteins in a vegetarian diet. Generally by consuming high-quality, animal-based products meat, milk, eggs, and cheese an individual will achieve optimal growth as compared to ingesting only plant proteins [ ].

Research has shown that soy is considered a lower quality complete protein. Hartman et al. They found that the participants that consumed the milk protein increased lean mass and decreased fat mass more than the control and soy groups.

Moreover, the soy group was not significantly different from the control group. Similarly, a study by Tang and colleagues [ 86 ] directly compared the abilities of hydrolyzed whey isolate, soy isolate, and micellar casein to stimulate rates of MPS both at rest and in response to a single bout of lower body resistance training.

These authors reported that the ability of soy to stimulate MPS was greater than casein, but less than whey, at rest and in response to an acute resistance exercise stimulus.

While soy is considered a complete protein, it contains lower amounts of BCAAs than bovine milk [ ]. Additionally, research has found that dietary soy phytoestrogens inhibit mTOR expression in skeletal muscle through activation of AMPK [ ].

Thus, not only does soy contain lower amounts of the EAAs and leucine, but soy protein may also be responsible for inhibiting growth factors and protein synthesis via its negative regulation of mTOR. When considering the multitude of plant sources of protein, soy overwhelmingly has the most research.

Limited evidence using wheat protein in older men has suggested that wheat protein stimulates significantly lower levels of MPS when compared to an identical dose 35 g of casein protein, but when this dose is increased nearly two fold 60 g this protein source is able to significantly increase rates of myofibrillar protein synthesis [ ].

As mentioned earlier, a study by Joy and colleagues [ 89 ] in which participants participated in resistance training program for eight weeks while taking identical, high doses of either rice or whey protein, demonstrated that rice protein stimulated similar increases in body composition adaptations to whey protein.

The majority of available science has explored the efficacy of ingesting single protein sources, but evidence continues to mount that combining protein sources may afford additional benefits [ ]. For example, a week resistance training study by Kerksick and colleagues [ 22 ] demonstrated that a combination of whey 40 g and casein 8 g yielded the greatest increase in fat-free mass determined by DEXA when compared to both a combination of 40 g of whey, 5 g of glutamine, and 3 g of BCAAs and a placebo consisting of 48 g of a maltodextrin carbohydrate.

Later, Kerksick et al. Similarly, Hartman and investigators [ 93 ] had 56 healthy young men train for 12 weeks while either ingesting isocaloric and isonitrogenous doses of fat-free milk a blend of whey and casein , soy protein or a carbohydrate placebo and concluded that fat-free milk stimulated the greatest increases in Type I and II muscle fiber area as well as fat-free mass; however, strength outcomes were not affected.

Moreover, Wilkinson and colleagues [ 94 ] demonstrated that ingestion of fat-free milk vs. soy or carbohydrate led to a greater area under the curve for net balance of protein and that the fractional synthesis rate of muscle protein was greatest after milk ingestion.

In , Reidy et al. However, when the entire four-hour measurement period was considered, no difference in MPS rates were found.

A follow-up publication from the same clinical trial also reported that ingestion of the protein blend resulted in a positive and prolonged amino acid balance when compared to ingestion of whey protein alone, while post-exercise rates of myofibrillar protein synthesis were similar between the two conditions [ ].

Reidy et al. No differences were found between whey and the whey and soy blend. Some valid criteria exist to compare protein sources and provide an objective method of how to include them in a diet. As previously mentioned, common means of assessing protein quality include Biological Value, Protein Efficiency Ratio, PDCAAS and IAAO.

The derivation of each technique is different with all having distinct advantages and disadvantages. For nearly all populations, ideal methods should be linked to the capacity of the protein to positively affect protein balance in the short term, and facilitate increases and decreases in lean and fat-mass, respectively, over the long term.

To this point, dairy, egg, meat, and plant-based proteins have been discussed. As mentioned previously, initial research by Boirie and Dangin has highlighted the impact of protein digestion rate on net protein balance with the two milk proteins: whey and casein [ , , ].

Subsequent follow-up work has used this premise as a reference point for the digestion rates of other protein sources. Using the criteria of leucine content, Norton and Wilson et al. Wheat and soy did not stimulate MPS above fasted levels, whereas egg and whey proteins significantly increased MPS rates, with MPS for whey protein being greater than egg protein.

MPS responses were closely related to changes in plasma leucine and phosphorylation of 4E—BP1 and S6 K protein signaling molecules. More importantly, following 2- and weeks of ingestion, it was demonstrated that the leucine content of the meals increased muscle mass and was inversely correlated with body fat.

Tang et al. These findings lead us to conclude that athletes should seek protein sources that are both fast-digesting and high in leucine content to maximally stimulate rates of MPS at rest and following training.

Moreover, in consideration of the various additional attributes that high-quality protein sources deliver, it may be advantageous to consume a combination of higher quality protein sources dairy, egg, and meat sources. Multiple protein sources are available for an athlete to consider, and each has their own advantages and disadvantages.

Protein sources are commonly evaluated based upon the content of amino acids, particularly the EAAs, they provide. Blends of protein sources might afford a favorable combination of key nutrients such as leucine, EAAs, bioactive peptides, and antioxidants, but more research is needed to determine their ideal composition.

Nutrient density is defined as the amount of a particular nutrient carbohydrate, protein, fat, etc. per unit of energy in a given food. In many situations, the commercial preparation method of foods can affect the actual nutrient density of the resulting food.

When producing milk protein supplements, special preparations must be made to separate the protein sources from the lactose and fat calories in milk. For example, the addition of acid to milk causes the casein to coagulate or collect at the bottom, while the whey is left on the top [ ].

These proteins are then filtered to increase their purity. Filtration methods differ, and there are both benefits and disadvantages to each. Ion exchange exposes a given protein source, such as whey, to hydrochloric acid and sodium hydroxide, thereby producing an electric charge on the proteins that can be used to separate them from lactose and fat [ ].

The advantage of this method is that it is relatively cheap and produces the highest protein concentration [ ]. The disadvantage is that ion exchange filtration typically denatures some of the valuable immune-boosting, anti-carcinogenic peptides found in whey [ ].

Cross-flow microfiltration, and ultra-micro filtration are based on the premise that the molecular weight of whey protein is greater than lactose, and use 1 and 0. As a result, whey protein is trapped in the membranes but the lactose and other components pass through.

The advantage is that these processes do not denature valuable proteins and peptides found in whey, so the protein itself is deemed to be of higher quality [ ]. The main disadvantage is that this filtration process is typically costlier than the ion exchange method.

When consumed whole, proteins are digested through a series of steps beginning with homogenization by chewing, followed by partial digestion by pepsin in the stomach [ ]. Following this, a combination of peptides, proteins, and negligible amounts of single amino acids are released into the small intestine and from there are either partially hydrolyzed into oligopeptides, 2—8 amino acids in length or are fully hydrolyzed into individual amino acids [ ].

Absorption of individual amino acids and various small peptides di, tri, and tetra into the blood occurs inside the small intestine through separate transport mechanisms [ ]. Oftentimes, products contain proteins that have been pre-exposed to specific digestive enzymes causing hydrolysis of the proteins into di, tri, and tetrapeptides.

A plethora of studies have investigated the effects of the degree of protein fractionation or degree of hydrolysis on the absorption of amino acids and the subsequent hormonal response [ , , , , , ]. Further, the rate of absorption may lead to a more favorable anabolic hormonal environment [ , , ].

Calbet et al. Each of the nitrogen containing solutions contained 15 g of glucose and 30 g of protein. Results indicated that peptide hydrolysates produced a faster increase in venous plasma amino acids compared to milk proteins.

Further, the peptide hydrolysates produced peak plasma insulin levels that were two- and four-times greater than that evoked by the milk and glucose solutions, respectively, with a correlation of 0.

In a more appropriate comparison, Morifuji et al. However, Calbet et al. The hydrolyzed casein, however, did result in a greater amino acid response than the nonhydrolyzed casein.

Finally, both hydrolyzed groups resulted in greater gastric secretions, as well as greater plasma increases, in glucose-dependent insulinotropic polypeptides [ ]. Buckley and colleagues [ ] found that a ~ 30 g dose of a hydrolyzed whey protein isolate resulted in a more rapid recovery of muscle force-generating capacity following eccentric exercise, compared with a flavored water placebo or a non-hydrolyzed form of the same whey protein isolate.

In agreement with these findings, Cooke et al. Three and seven days after completing the damaging exercise bout, maximal strength levels were higher in the hydrolyzed whey protein group compared to carbohydrate supplementation. Additionally, blood concentrations of muscle damage markers tended to be lower when four ~g doses of a hydrolyzed whey protein isolate were ingested for two weeks following the damaging bout.

Beyond influencing strength recovery after damaging exercise, other benefits of hydrolyzed proteins have been suggested. For example, Morifuji et al. Furthermore, Lockwood et al. Results indicated that strength and lean body mass LBM increased equally in all groups.

However, fat mass decreased only in the hydrolyzed whey protein group. While more work needs to be completed to fully determine the potential impact of hydrolyzed proteins on strength and body composition changes, this initial study suggests that hydrolyzed whey may be efficacious for decreasing body fat.

Finally, Saunders et al. The authors reported that co-ingestion of a carbohydrate and protein hydrolysate improved time-trial performance late in the exercise protocol and significantly reduced soreness and markers of muscle damage. Two excellent reviews on the topic of hydrolyzed proteins and their impact on performance and recovery have been published by Van Loon et al.

The prevalence of digestive enzymes in sports nutrition products has increased during recent years with many products now containing a combination of proteases and lipases, with the addition of carbohydrates in plant proteins. Proteases can hydrolyze proteins into various peptide configurations and potentially single amino acids.

It appears that digestive enzyme capabilities and production decrease with age [ ], thus increasing the difficulty with which the body can break down and digest large meals. Digestive enzymes could potentially work to promote optimal digestion by allowing up-regulation of various metabolic enzymes that may be needed to allow for efficient bodily operation.

Further, digestive enzymes have been shown to minimize quality differences between varying protein sources [ ]. Individuals looking to increase plasma peak amino acid concentrations may benefit from hydrolyzed protein sources or protein supplemented with digestive enzymes.

However, more work is needed before definitive conclusions can be drawn regarding the efficacy of digestive enzymes.

Despite a plethora of studies demonstrating safety, much concern still exists surrounding the clinical implications of consuming increased amounts of protein, particularly on renal and hepatic health.

The majority of these concerns stem from renal failure patients and educational dogma that has not been rewritten as evidence mounts to the contrary. Certainly, it is clear that people in renal failure benefit from protein-restricted diets [ ], but extending this pathophysiology to otherwise healthy exercise-trained individuals who are not clinically compromised is inappropriate.

Published reviews on this topic consistently report that an increased intake of protein by competitive athletes and active individuals provides no indication of hepato-renal harm or damage [ , ].

This is supported by a recent commentary [ ] which referenced recent reports from the World Health Organization [ ] where they indicated a lack of evidence linking a high protein diet to renal disease. Likewise, the panel charged with establishing reference nutrient values for Australia and New Zealand also stated there was no published evidence that elevated intakes of protein exerted any negative impact on kidney function in athletes or in general [ ].

Recently, Antonio and colleagues published a series of original investigations that prescribed extremely high amounts of protein ~3. The first study in had resistance-trained individuals consume an extremely high protein diet 4.

A follow-up investigation [ ] required participants to ingest up to 3. Their next study employed a crossover study design in twelve healthy resistance-trained men in which each participant was tested before and after for body composition as well as blood-markers of health and performance [ ].

In one eight-week block, participants followed their normal habitual diet 2. No changes in body composition were reported, and importantly, no clinical side effects were observed throughout the study.

Finally, the same group of authors published a one-year crossover study [ ] in fourteen healthy resistance-trained men. This investigation showed that the chronic consumption of a high protein diet i. Furthermore, there were no alterations in clinical markers of metabolism and blood lipids.

Multiple review articles indicate that no controlled scientific evidence exists indicating that increased intakes of protein pose any health risks in healthy, exercising individuals. A series of controlled investigations spanning up to one year in duration utilizing protein intakes of up to 2.

In alignment with our previous position stand, it is the position of the International Society of Sports Nutrition that the majority of exercising individuals should consume at minimum approximately 1.

The amount is dependent upon the mode and intensity of the exercise, the quality of the protein ingested, as well as the energy and carbohydrate status of the individual. Concerns that protein intake within this range is unhealthy are unfounded in healthy, exercising individuals.

An attempt should be made to consume whole foods that contain high-quality e. The timing of protein intake in the period encompassing the exercise session may offer several benefits including improved recovery and greater gains in lean body mass. In addition, consuming protein pre-sleep has been shown to increase overnight MPS and next-morning metabolism acutely along with improvements in muscle size and strength over 12 weeks of resistance training.

Intact protein supplements, EAAs and leucine have been shown to be beneficial for the exercising individual by increasing the rates of MPS, decreasing muscle protein degradation, and possibly aiding in recovery from exercise.

In summary, increasing protein intake using whole foods as well as high-quality supplemental protein sources can improve the adaptive response to training.

Campbell B, Kreider RB, Ziegenfuss T, La Bounty P, Roberts M, Burke D, et al. International society of sports nutrition position stand: protein and exercise. J Int Soc Sports Nutr. Macdermid PW, Stannard SR.

A whey-supplemented, high-protein diet versus a high-carbohydrate diet: effects on endurance cycling performance. Int J Sport Nutr Exerc Metab. Article CAS PubMed Google Scholar. Burke LM, Hawley JA, Wong SH, Jeukendrup AE. Carbohydrates for training and competition. J Sports Sci. Article PubMed Google Scholar.

Witard OC, Jackman SR, Kies AK, Jeukendrup AE, Tipton KD. Effect of increased dietary protein on tolerance to intensified training. Med Sci Sports Exerc. D'lugos AC, Luden ND, Faller JM, Akers JD, Mckenzie AI, Saunders MJ. Supplemental protein during heavy cycling training and recovery impacts skeletal muscle and heart rate responses but not performance.

Article CAS Google Scholar. Breen L, Tipton KD, Jeukendrup AE. No effect of carbohydrate-protein on cycling performance and indices of recovery. CAS PubMed Google Scholar. Saunders MJ, Moore RW, Kies AK, Luden ND, Pratt CA. Carbohydrate and protein hydrolysate coingestions improvement of late-exercise time-trial performance.

Valentine RJ, Saunders MJ, Todd MK, St Laurent TG.

How Much Iin Do Athletes Really Need? Los for both endurance and power athletes. Contents Losz Protein Atnletes Protein Requirements for Protein for weight loss in athletes Energy Restriction Rapid water weight loss Timing Main Takeaways About the Author References Comments Determining Protein Read more. By Alex St. John Last updated: June 25th, 15 min read. Many of those reading this will be aware of the general recommendation of 1 gram g of protein per pound lb of body mass

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How much protein do you need per day? To Build Muscle? To Lose Weight?