Hormonal Changes — Adequate protein intake can increase the release of the hormone glucagon. The release of glucagon counteracts the effects of insulin, facilitating the fat-burning process. Testing and Safety of Protein Powders Athletes also commonly ask about the best brand of protein powder to maximize muscle growth and recovery.

To ensure your product has been 3rd party tested, be sure to visit one of the following websites from the top agencies in the United States: NSF - www. com Informed Choice — www. org Banned Substance Control Group — www.

org How Much Protein Do You Need? Download Infographic. Another Athlete Another Athletic Trainer Another Coach Another Dietitian Another Parent Another Strength Coach Blog Conference or Clinic Google Search Podcast Social Media Ad. Share Post Share Pin it. Links and Resources Increasing Protein for Athletes Dietary Supplement University Informed Choice Certified: Trusted by Sport Supplements: Do I Really Need Them?

Drug Supplement Testing in Sports Optimizing Protein Intake for Athletes High Protein Diet in Athletes Sports Nutrition for Power Athletes Dietary Supplements and Athletic Performance Supplement Industry and Supplement Safety.

Facebook comments. The 9 essential amino acids therefore must be obtained through the diet since the body has no internal source of them. They serve many vital functions such as in metabolism, cellular signaling, enzymes and cell structure and function such as in muscle.

One way to increase this free pool of amino acids is through an increase in dietary protein intake. The US Food and Nutrition Board recommends 0. This number was carefully obtained through scientific research. This is about 65 g of protein per day for a lb person, or the equivalent of about 2½ 4 oz boneless skinless chicken breasts.

There has been recent thought however that the protein requirements in an athlete may be greater than this recommendation depending on the specific type of athletic activity and training goals. As recommended recently by the American College of Sports Medicine, endurance athletes should maintain an increased dietary protein intake of 1.

In athletes that train at higher intensities or for long periods of time, the required amount of protein may be even slightly higher as suggested in some studies. The benefit of higher dietary amino acid intake in endurance athletes has been debated beyond simply balancing the amount of nitrogen in the body for protein composition.

This causes a secondary increase in tryptophan levels that in turn can cause a depressive affect on the central nervous system leading to a decrease in athletic performance.

Another theory regarding the benefit of increasing dietary protein intake in endurance athletes is their role in exercise recovery.

Again no definitive proof exists that demonstrates a benefit in athletic performance. However, there is some evidence that creatine kinase and lactic acid levels decrease with amino acid supplementation both of which have been correlated with delayed onset muscle soreness.

There is also a suggested decrease in the rate of infections through a similar mechanism. Amino acid intake and protein synthesis has long been a topic in the forefront in the setting of the strength training athlete.

Resistance exercise is followed by a 48 hour period when muscle protein synthesis is elevated. Protein synthesis is necessary for an increase in muscle mass and therefore an increased dietary intake of amino acids is suggested. Some studies suggest that the daily dietary protein intake in weight-training athletes is between 1.

While the short term data available does not clearly confer that an increased dietary protein intake improves strength, there has been this suggestion. It is possible that longer term duration studies of strength athletes may prove an increased measured strength with increased dietary protein and amino acid supplementation.

It is however clear that there is a limit on the amount of protein synthesis and therefore muscle building potential is based on oral protein intake.

Protein or amino acids ingested above this limit will not induce further protein synthesis. Furthermore, there may be an increased protein requirement during early muscle building periods when an athlete is training to build muscle mass.

However, most athletes reach a phase in their training when they are no longer increasing muscle mass and instead are maintaining a high, but stable level of muscle mass.

During this stable muscle mass period, protein requirements may be elevated somewhat above normal requirements due to a small increase in resting muscle protein turnover.

Research studies have suggested that this level is increased to 0. Despite all the academic debate over the proposed benefits of oral protein supplementation based on protein synthesis and nitrogen balance, the true measuring stick is athletic performance.

Supplemental protein intake is unnecessary for most athletes as long as they consume a healthy diet containing complete protein foods, and it meets their energy needs. There are risk factors for athletes that do not have a sufficient dietary protein intake including vegetarians, athletes in weight-class competition sports, those with insufficient energy intake, sudden increases in training intensity and athletes in weight loss programs.

Vegetarian athletes are at a higher risk of protein deficiency than other athletes. 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. Influence of carbohydrate-protein beverage on cycling endurance and indices of muscle disruption.

Van Essen M, Gibala MJ. Failure of protein to improve time trial performance when added to a sports drink. Article PubMed CAS Google Scholar.

Ivy JL, Res PT, Sprague RC, Widzer MO. Effect of a carbohydrate-protein supplement on endurance performance during exercise of varying intensity. Saunders MJ, Kane MD, Todd MK. Effects of a carbohydrate-protein beverage on cycling endurance and muscle damage.

Saunders MJ, Luden ND, Herrick JE. Consumption of an oral carbohydrate-protein gel improves cycling endurance and prevents postexercise muscle damage.

J Strength Cond Res. PubMed Google Scholar. Romano-Ely BC, Todd MK, Saunders MJ, Laurent TS. Effect of an isocaloric carbohydrate-protein-antioxidant drink on cycling performance. Beelen M, Zorenc A, Pennings B, Senden JM, Kuipers H, Van Loon LJ. Impact of protein coingestion on muscle protein synthesis during continuous endurance type exercise.

Am J Physiol Endocrinol Metab. Andersen LL, Tufekovic G, Zebis MK, Crameri RM, Verlaan G, Kjaer M, et al. The effect of resistance training combined with timed ingestion of protein on muscle fiber size and muscle strength.

Metab Clin Exp. Bemben MG, Witten MS, Carter JM, Eliot KA, Knehans AW, Bemben DA. The effects of supplementation with creatine and protein on muscle strength following a traditional resistance training program in middle-aged and older men.

J Nutr Health Aging. Burke DG, Chilibeck PD, Davidson KS, Candow DG, Farthing J, Smith-Palmer T. The effect of whey protein supplementation with and without creatine monohydrate combined with resistance training on lean tissue mass and muscle strength.

Denysschen CA, Burton HW, Horvath PJ, Leddy JJ, Browne RW. Resistance training with soy vs whey protein supplements in hyperlipidemic males. Article PubMed PubMed Central CAS Google Scholar. Erskine RM, Fletcher G, Hanson B, Folland JP.

Whey protein does not enhance the adaptations to elbow flexor resistance training. Herda AA, Herda TJ, Costa PB, Ryan ED, Stout JR, Cramer JT. Muscle performance, size, and safety responses after eight weeks of resistance training and protein supplementation: a randomized, double-blinded, placebo-controlled clinical trial.

Hulmi JJ, Kovanen V, Selanne H, Kraemer WJ, Hakkinen K, Mero AA. Acute and long-term effects of resistance exercise with or without protein ingestion on muscle hypertrophy and gene expression.

Amino Acids. Kerksick CM, Rasmussen CJ, Lancaster SL, Magu B, Smith P, Melton C, et al. The effects of protein and amino acid supplementation on performance and training adaptations during ten weeks of resistance training.

Kukuljan S, Nowson CA, Sanders K, Daly RM. Effects of resistance exercise and fortified milk on skeletal muscle mass, muscle size, and functional performance in middle-aged and older men: an mo randomized controlled trial.

J Appl Physiol Bethesda, Md : Weisgarber KD, Candow DG, Vogt ES. Whey protein before and during resistance exercise has no effect on muscle mass and strength in untrained young adults. Willoughby DS, Stout JR, Wilborn CD.

Effects of resistance training and protein plus amino acid supplementation on muscle anabolism, mass, and strength. Candow DG, Burke NC, Smith-Palmer T, Burke DG. Effect of whey and soy protein supplementation combined with resistance training in young adults.

Cribb PJ, Williams AD, Stathis CG, Carey MF, Hayes A. Effects of whey isolate, creatine, and resistance training on muscle hypertrophy. Hoffman JR, Ratamess NA, Kang J, Falvo MJ, Faigenbaum AD. Article PubMed PubMed Central Google Scholar.

Effects of protein supplementation on muscular performance and resting hormonal changes in college football players. J Sports Sci Med. PubMed PubMed Central Google Scholar. Hida A, Hasegawa Y, Mekata Y, Usuda M, Masuda Y, Kawano H, et al.

Effects of egg white protein supplementation on muscle strength and serum free amino acid concentrations. Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, et al.

Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr.

Schoenfeld BJ, Aragon AA, Krieger JW. The effect of protein timing on muscle strength and hypertrophy: a meta-analysis. Josse AR, Tang JE, Tarnopolsky MA, Phillips SM. Body composition and strength changes in women with milk and resistance exercise. Taylor LW, Wilborn C, Roberts MD, White A, Dugan K.

Eight weeks of pre- and postexercise whey protein supplementation increases lean body mass and improves performance in division III collegiate female basketball players.

Appl Physiol Nutr Metab. Cermak NM, Res PT, De Groot LC, Saris WH, Van Loon LJ. Protein supplementation augments the adaptive response of skeletal muscle to resistance-type exercise training: a meta-analysis.

Pasiakos SM, Mclellan TM, Lieberman HR. The effects of protein supplements on muscle mass, strength, and aerobic and anaerobic power in healthy adults: a systematic review. Sports Med.

Rennie MJ. Control of muscle protein synthesis as a result of contractile activity and amino acid availability: implications for protein requirements. Phillips SM. The science of muscle hypertrophy: making dietary protein count. Proc Nutr Soc.

Tipton KD, Phillips SM. Dietary protein for muscle hypertrophy. Nestle Nutrition Institute workshop series. Layman DK, Evans E, Baum JI, Seyler J, Erickson DJ, Boileau RA.

Dietary protein and exercise have additive effects on body composition during weight loss in adult women. J Nutr. Layman DK, Boileau RA, Erickson DJ, Painter JE, Shiue H, Sather C, et al. A reduced ratio of dietary carbohydrate to protein improves body composition and blood lipid profiles during weight loss in adult women.

Pasiakos SM, Cao JJ, Margolis LM, Sauter ER, Whigham LD, Mcclung JP, et al. Effects of high-protein diets on fat-free mass and muscle protein synthesis following weight loss: a randomized controlled trial.

FASEB J. Kerksick C, Thomas A, Campbell B, Taylor L, Wilborn C, Marcello B, et al. Effects of a popular exercise and weight loss program on weight loss, body composition, energy expenditure and health in obese women.

Nutr Metab Lond. Kerksick CM, Wismann-Bunn J, Fogt D, Thomas AR, Taylor L, Campbell BI, et al. Changes in weight loss, body composition and cardiovascular disease risk after altering macronutrient distributions during a regular exercise program in obese women.

Nutr J. Kreider RB, Serra M, Beavers KM, Moreillon J, Kresta JY, Byrd M, et al. A structured diet and exercise program promotes favorable changes in weight loss, body composition, and weight maintenance.

J Am Diet Assoc. Biolo G, Tipton KD, Klein S, Wolfe RR. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein.

Am J Phys. CAS Google Scholar. Zawadzki KM, Yaspelkis BB 3rd, Ivy JL. Carbohydrate-protein complex increases the rate of muscle glycogen storage after exercise. J Appl Physiol. Bethesda, Md : Biolo G, Maggi SP, Williams BD, Tipton KD, Wolfe RR. Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans.

Tipton KD, Ferrando AA, Phillips SM, Doyle D Jr, Wolfe RR. Postexercise net protein synthesis in human muscle from orally administered amino acids. Burd NA, West DW, Moore DR, Atherton PJ, Staples AW, Prior T, et al.

Enhanced amino acid sensitivity of myofibrillar protein synthesis persists for up to 24 h after resistance exercise in young men.

Tipton KD, Gurkin BE, Matin S, Wolfe RR. Nonessential amino acids are not necessary to stimulate net muscle protein synthesis in healthy volunteers. J Nutr Biochem. Borsheim E, Tipton KD, Wolf SE, Wolfe RR. Essential amino acids and muscle protein recovery from resistance exercise.

Volpi E, Kobayashi H, Sheffield-Moore M, Mittendorfer B, Wolfe RR. Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults.

CAS PubMed PubMed Central Google Scholar. Tipton KD, Rasmussen BB, Miller SL, Wolf SE, Owens-Stovall SK, Petrini BE, et al. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise.

Tipton KD, Borsheim E, Wolf SE, Sanford AP, Wolfe RR. Acute response of net muscle protein balance reflects h balance after exercise and amino acid ingestion. Coffey VG, Moore DR, Burd NA, Rerecich T, Stellingwerff T, Garnham AP, et al.

Nutrient provision increases signalling and protein synthesis in human skeletal muscle after repeated sprints.

Eur J Appl Physiol. Breen L, Philp A, Witard OC, Jackman SR, Selby A, Smith K, et al. The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis. J Physiol. Ferguson-Stegall L, Mccleave EL, Ding Z, Doerner PG 3rd, Wang B, Liao YH, et al.

Postexercise carbohydrate-protein supplementation improves subsequent exercise performance and intracellular signaling for protein synthesis.

Volek JS. Influence of nutrition on responses to resistance training. Kerksick C, Harvey T, Stout J, Campbell B, Wilborn C, Kreider R, et al. International society of sports nutrition position stand: nutrient timing. Elliot TA, Cree MG, Sanford AP, Wolfe RR, Tipton KD.

Milk ingestion stimulates net muscle protein synthesis following resistance exercise. Farnfield MM, Breen L, Carey KA, Garnham A, Cameron-Smith D. Activation of mtor signalling in young and old human skeletal muscle in response to combined resistance exercise and whey protein ingestion.

Tang JE, Manolakos JJ, Kujbida GW, Lysecki PJ, Moore DR, Phillips SM. Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men.

Tipton KD. Role of protein and hydrolysates before exercise. Hulmi JJ, Kovanen V, Lisko I, Selanne H, Mero AA. The effects of whey protein on myostatin and cell cycle-related gene expression responses to a single heavy resistance exercise bout in trained older men. Ivy JL, Ding Z, Hwang H, Cialdella-Kam LC, Morrison PJ.

Post exercise carbohydrate-protein supplementation: Phosphorylation of muscle proteins involved in glycogen synthesis and protein translation.

Churchward-Venne TA, Murphy CH, Longland TM, Phillips SM. Role of protein and amino acids in promoting lean mass accretion with resistance exercise and attenuating lean mass loss during energy deficit in humans.

Short-term training: when do repeated bouts of resistance exercise become training? Can J Appl Physiol. Pennings B, Koopman R, Beelen M, Senden JM, Saris WH, Van Loon LJ.

Exercising before protein intake allows for greater use of dietary protein-derived amino acids for de novo muscle protein synthesis in both young and elderly men. Miller BF, Olesen JL, Hansen M, Dossing S, Crameri RM, Welling RJ, et al. Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise.

Camera DM, Edge J, Short MJ, Hawley JA, Coffey VG. Early time course of akt phosphorylation after endurance and resistance exercise. Cribb PJ, Hayes A. Effects of supplement timing and resistance exercise on skeletal muscle hypertrophy.

Esmarck B, Andersen JL, Olsen S, Richter EA, Mizuno M, Kjaer M. Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans. Article CAS PubMed PubMed Central Google Scholar. Hoffman JR, Ratamess NA, Tranchina CP, Rashti SL, Kang J, Faigenbaum AD.

Effect of protein-supplement timing on strength, power, and body-composition changes in resistance-trained men. Fujita S, Dreyer HC, Drummond MJ, Glynn EL, Volpi E, Rasmussen BB. Essential amino acid and carbohydrate ingestion before resistance exercise does not enhance postexercise muscle protein synthesis.

J Appl Physiol Bird SP, Tarpenning KM, Marino FE. Roberts MD, Dalbo VJ, Hassell SE, Brown R, Kerksick CM. Effects of preexercise feeding on markers of satellite cell activation. Dalbo VJ, Roberts MD, Hassell S, Kerksick CM. Effects of pre-exercise feeding on serum hormone concentrations and biomarkers of myostatin and ubiquitin proteasome pathway activity.

Eur J Nutr. Tipton KD, Elliott TA, Cree MG, Wolf SE, Sanford AP, Wolfe RR.

A plant-based vegetarian diet can supply all essential and nonessential amino acid requirements for protein synthesis. Vegan athletes are at further risk of protein insufficiency because their diets lack animal protein sources altogether. There is also some concern that protein from plant-based sources is used less effectively by the body than protein from animal sources.

Although both vegetarian and vegan diets can provide sufficient protein, if this is not the case, then additional dietary or supplemental protein could be considered. In fact, energy intake may have as significant an affect on protein requirements as does the amount of dietary protein itself.

Athletes can gain strength and maintain muscle mass even when dietary protein intake is low if energy intake is sufficient. With strength training, a positive energy balance is more important than increased protein for stimulating gains in lean body mass.

Therefore, athletes that restrict energy intake must be especially conscious of their dietary protein intake. This often includes athletes in weight class sports like wrestling and boxing as well as those in sports at risk for eating disorders like gymnastics, long distance running and figure skating.

There are also potential performance drawbacks for athletes to energy restriction in high protein diets. A recent research study demonstrated that the performance of well-trained cyclists was impaired on a high protein, low carbohydrate diet. Comprised carbohydrate intake with higher protein intake may cause glycogen levels to be reduced.

Subsequently athletes whose training involves high intensity or prolonged workouts may suffer. Creatine, widely used as an ergonomic supplement since the early s, is a common protein synthesized in the liver from the amino acids glycine and arginine.

The great majority of creatine is found in the liver, however some creatine is also seen in the heart, brain and other organs. Creatine is abundant in meat and fish and as more creatine is ingested in the diet, the less is necessary to be provided by the liver.

Creatine in muscle becomes creatine kinase by the addition of phosphorous phosphorylation and then is a source of ATP adenosine triphosphate — the main basic energy source used by the body.

The ATP located within muscle provides energy during intense, quick repeated bursts of exercise seen in some competitive sports as well as strength training. Dietary supplementation is widely promoted to provide muscle with and increased level of creatine.

In theory, higher creatine levels in muscle will allow for improved ability to produce energy during and recover quicker from high intensity exercise. The performance effects of creatine supplementation have been researched widely.

There is an increase seen in total body mass along with greater gains in strength, fat-free mass and sprinting performance. No improvement in aerobic performance occurs during endurance training as normal ATP production provides sufficient ATP in this circumstance.

For healthy athletes with no history of kidney disease, creatine is a safe product taken as a short-term supplement. Creatine supplementation is thought to lead to dehydration, however this has not been a problem in healthy athletes.

Athletes with a history of kidney disease should be cautioned about possible side effects of excessive oral creatine intake because creatine and its metabolites are processed in the kidneys.

Longer term effects of creatine supplementation are not well known. Armsey TD Jr, Grime TE. Protein and amino Acid supplementation in athletes.

Curr Sports Med Rep. Phillips SM. Protein requirements and supplementation in strength sports. Nemet D, Wolach B, Eliakim A. Proteins and amino acid supplementation in sports: are they truly necessary? Isr Med Assoc J. Kevin D. Tipton, PhD, Oliver C. Witard, MSc. Protein Requirements and Recommendations for Athletes: Relevance of Ivory Tower Arguments for Practical RecommendationsClin Sports Med 26 17— John M.

Tokish, Mininder S. Kocher and Richard J. Ergogenic Aids: A Review of Basic Science, Performance, Side Effects, and Status in Sports. Am J Sports Med Protein Supplementation in Athletes By Scott Kaar, MD What are proteins and their building blocks?

What are the recommended protein requirements? What is the role of amino acids and the endurance athlete? Protein is an essential nutrient in the diet and getting enough protein is important for everyone; especially athletes.

But why does it play such a key role? Here, we give you all the need-to-knows on this essential nutrient, discussing its importance for the body, athletic performance and practical ways to achieve protein targets.

Protein makes up the structure of cells and tissues in the body, including muscle tissue. Although the majority of energy comes from carbohydrates and fat during exercise, protein may also contribute to fuelling exercise.

Protein is needed for the growth and formation of new tissue, and it also helps to repair any muscle fibres that may have been damaged through exercise.

As well as this, protein plays a role in making various enzymes and hormones - such as adrenaline — whilst also maintaining fluid balances in tissue when transporting important nutrients around the body and regulating blood clotting. It is well researched that consuming protein after exercises increases post-training adaptation and can help to enhance performance for both strength and endurance exercise.

However, how much protein you consume in a serving is an ongoing debate in research. Most believe that 0. Amino acids are building blocks of proteins that are combined in many ways to make a protein. It is the amount of these essential amino acids that determine the usefulness of the protein in the body.

However, plant sources such as beans, lentils, nuts, grains and seeds are protein sources that lack in one or more essentials amino acids. a portion of beans and rice. Milk-based proteins, such as whey and casein, have been shown to promote greater protein uptake in the muscle and should therefore be seriously considered as supplements by athletes across many disciplines.

These are the bases of our two best-selling protein shake formulas; Big Whey whey and Nighttime Protein casein. Both large gaps during the day without protein and not consuming enough protein are common issues among athletes.

As mentioned, protein should be evenly spread throughout the day with 20g per meal and particularly post-exercise. Here are some easy go-to foods that can help you achieve these targets:. This site will not work correctly when cookies are disabled.