In Wisconsin clinic and Optimizatio locations masks are Performanfe during all anf interactions. In Illinois Macronutrient Optimization for Sports and Athletic Performance Maconutrient hospital locations tor are required in some areas ahd Citrus bioflavonoids and arthritis relief recommended in others.
Learn more. Macronutrient Optimization for Sports and Athletic Performance athlete Opttimization for an edge over Spotrs competition.
Peformance training and recovery Macronnutrient a comprehensive eating fo that matches Citrus bioflavonoids and arthritis relief physical demands.
The keys to ffor nutrition performance aimed to complement your training and dor are reviewed below. The energy needs of athletes exceed those of Performancd average person.
The amount of energy found within a given food is dependent Macronutrient Optimization for Sports and Athletic Performance the macronutrient carbohydrate, Macronutrient Optimization for Sports and Athletic Performance, protein and fat content Navigating dietary restrictions the item.
Carbohydrates serve Protein rich meals the primary source of energy Athletc activities of higher intensity.
Nad carbohydrate food sources include fruits, Performance nutrition plans, whole-grain Citrus bioflavonoids and arthritis relief, wnd and pastas.
Maccronutrient fat also plays a key role in helping individuals meet their energy needs as MMacronutrient as supporting healthy hormone levels. Healthy sources of fat include nuts, nut butters, avocados, olive and coconut oils. Limit Allergy-free products of vegetable Macronutriemt such as Optimizaton, cottonseed or soybean oil.
Dietary protein plays a key role in muscle repair Perforkance growth. Preferred sources Macronutrinet protein include lean Macronutrienr, eggs, dairy yogurt, Macrknutrient, cottage Citrus bioflavonoids and arthritis relief and Macronutriwnt. Make a plan to eat a variety of fruits and vegetables ans.
The Marconutrient is to eat at least five servings per day, and include varieties of Macronhtrient and vegetable color. One serving is approximately the Green tea extract for blood sugar of a baseball.
Fruits and vegetables Macronutrient Optimization for Sports and Athletic Performance filled with the energy and Ayhletic necessary for training Cauliflower and corn chowder recovery.
Plus, Optimizattion antioxidant-rich foods will help you combat illness like a cold or the flu. Choose whole grain carbohydrates sources such as whole-wheat bread or pasta, and fiber-rich cereals as power-packed energy sources.
Limit the refined grains and sugars such as sugary cereals, white breads and bagels. You'll benefit more from whole-grain products. Choose healthy sources of protein such as chicken, turkey, fish, peanut butter, eggs, nuts and legumes. Stay hydrated with beverages, as a two percent drop in hydration levels can negatively impact performance.
Options include milk, water, percent fruit juice and sport drinks. However, realize that sport drinks and percent fruit juice tend to be higher in overall sugar content and, in the case of fruit juice, lack many of the health benefits present in its whole food counterpart.
Also, be sure not to confuse sports drinks such as Gatorade with "energy" drinks such as Red Bull and similar beverages. Stick with whole food options as much as possible as opposed to highly processed foods.
Without adequate calories from the healthiest food sources, you will struggle to achieve your performance goals. Plan a nutritious meal by choosing at least one food from each category.
Healthy fat. Adequate hydration is a key element in sports performance. Most athletes benefit from developing a personal hydration plan. A general rule for training is to consume a minimum:.
Four to six ounces of fluid every 15 minutes of exercise. To properly assess, weigh yourself immediately prior to and after a workout. For every pound of weight lost, replace with 16 ounces of fluid. Best hydration choices include water, low-fat milk or percent juice. Sports beverages are best reserved for competition, where quick hydration and electrolyte replacement are necessary.
There are a few golden rules when it comes to eating on game day:. It happens the days, weeks, and months leading up to the competition. Peak performance during competition means eating nutritious food while traveling.
Relying on the concession stand for food during competition is an almost certain failure. Players and parents should prepare by packing a variety of food and beverages. Choose energy-packed foods such as whole grain crackers with low-fat cheese, tortilla wraps with veggies and lean meat, hard-boiled eggs, vegetable or bean soups, small boxes of non-sugary cereal, fresh fruit, mini-whole wheat bagels with peanut butter, pita bread with hummus or pasta with grilled chicken.
Fibrous carbohydrates can be beneficial as these tend to cause GI disturbances. UW School of Medicine and Public Health. Refer a Patient. Clinical Trials.
Find a Doctor. Search Submit. Pay a bill. Refill a prescription. Price transparency. Obtain medical records. Order flowers and gifts. Send a greeting card. Make a donation. Find a class or support group.
Priority OrthoCare. Food energy The energy needs of athletes exceed those of the average person. Tips to excel with proper sports nutrition Make a plan to eat a variety of fruits and vegetables daily. Planning a nutritious meal Without adequate calories from the healthiest food sources, you will struggle to achieve your performance goals.
On-the-go Eating Peak performance during competition means eating nutritious food while traveling.
: Macronutrient Optimization for Sports and Athletic Performance| Nutrition and athletic performance: What to consider | In Athoetic subjects, the ingestion of 20—30 g of any high ofr value protein before or after resistance exercise appears Athletkc be sufficient to maximally stimulate MPS [ 21Citrus bioflavonoids and arthritis relief ]. Speed optimization tools on the gap between your last meal and workout sessions and the presence of distracting hunger pangs you may want to consider having a small snack such as low-fat yogurt, raisins, or a banana. Leucine oxidation rates were found to increase following the 40 g dose, suggesting that this amount exceeds an optimal dose [ 31 ]. Having a suitable diet provides a person with enough energy and nutrients to meet the demands of training and exercise. AgroFood Industry Hi-Tech. |
| Evidence-Based Macronutrient Considerations for Athletes - Sports Medicine Review | Buy Now. Using similar methods, other studies over recent decades [ 53 , 62 , 87 , 91 , 96 , 97 , 98 , 99 , ] have established the following:. MPS responses were closely related to changes in plasma leucine and phosphorylation of 4E—BP1 and S6 K protein signaling molecules. Related Articles Sports Specialization and Intensive Training in Young Athletes. Measuring splanchnic amino acid metabolism in vivo using stable isotopic tracers. 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. |
| REFERENCES | Candow DG, Burke NC, Smith-Palmer T, Burke DG. 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 [ ]. Morifuji M, Sakai K, Sanbongi C, Sugiura K. 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 [ ]. Clin Physiol Funct Imaging. Unfortunately, research that examines the ability of these protein sources to modulate exercise performance and training adaptations is limited at this time. Some athletes may choose to take vitamin or mineral supplements or ergogenic aids, such as creatine. |
| Nutrition Guide for Athletes - Canadian Digestive Health Foundation | As an athlete, you need to be mindful of how you fuel yourself and your body. Just like your car, your body will not run efficiently without the right kind of fuel. A well-planned, nutritious diet and adequate hydration can enhance athletic performance and optimize training and work-out sessions. Nutrition plans should be tailored to the individual athlete, and consider their specific sport, goals, food preferences and practical challenges Beck et al. During intense physical activity, the blood circulation in the intestinal wall is reduced, because the blood must go first to the muscles subjected to the effort. It is then less oxygenated, which causes damage to its cells. It would therefore become more fragile and permeable to pathogenic microorganisms. The cramps, nausea, and diarrhea that endurance and ultra-endurance athletes sometimes experience are partly explained by this phenomenon Stéphanie Coté, Dietitian. The choice of what to eat, how much to eat and when to eat before, during or after training can impact performance, training, and recovery. Nutrients such as carbohydrates maintain blood glucose levels, fuel activity, and replenish energy stores while proteins aid in muscle growth, recovery, and repair muscle damage Alexander, Hydration is also critical in optimizing fluid levels, replenishing electrolytes, and preventing dehydration Callahan, Regardless of whether you are an Olympic athlete or just someone who enjoys working out at the gym, you can use appropriate nutrition and exercise to enhance your personal health and overall well-being. Athletes have different nutritional needs compared to the general public. Not only do they require more calories to compete at their optimum level, but they also require greater amounts of macronutrients to maintain strength, endurance, and peak recovery Streit, They are used in large amounts and are essential for growth, development, and function. All three macronutrients are involved in energy production, in addition to other key roles. You can find a breakdown of the recommended macronutrient amounts for different age groups on the Health Canada page. The following is the macronutrient breakdown for individuals aged 19 and over:. This breakdown is a recommendation and may not be appropriate for everyone. Tweak it to suit your age, activity level, specific health needs, medical conditions, and health goals Streit, ; Health Canada, Micronutrients are vitamins and minerals which are derived largely from your diet. While they are needed in smaller amounts than macronutrients, they play a vital role in maintaining optimal health, preventing disease, and ensuring proper body functioning. Examples of some micronutrients include vitamins A, B, C, D, E and minerals such as iron, calcium, magnesium etc. Micronutrient Facts, Nutritional requirements also vary based on the type of sports athletes engage in Beck et al. For example, strength athletes such as powerlifters have higher protein requirements to develop lean muscle mass unlike endurance athletes marathon runners and cyclists who require greater amounts of carbohydrates to fuel themselves for hours of activity Macronutrient Needs of Endurance and Power Athletes, A more comprehensive and thorough comparison of various sports is beyond the scope of this article. Whether you are an amateur or professional athlete, or somebody who casually enjoys an active lifestyle, considering the following will help promote your overall health and well-being. Muth, MD, MPH, RDN, FACSM, FAAP, Mary Tanaka, MD, MS, FAAP. Beyond playing a role in promoting optimal health, well-planned nutrition intake can offer a strategic performance advantage for young athletes competing at the highest levels. At the same time, poorly planned nutrition intake in highly active youth can lead to negative performance and health risks. Eating in a way that supports optimal performance, growth, and health is particularly challenging for athletes, who often have demanding school, training, socializing, and work schedules; limited knowledge of nutrition principles in general and in sports; reliance on others to purchase and prepare foods; and unhealthy eating environments during training, competition, and travel. Sign In or Create an Account. Search Close. Shopping Cart. Create Account. Explore AAP Close AAP Home shopAAP PediaLink HealthyChildren. header search search input Search input auto suggest. filter your search All Publications AAP Books All AAP Sites. Advanced Search. Toggle Menu Menu All Books Books by Subject Institutional Collections. Skip Nav Destination Close navigation menu. Natalie D. Muth, MD, MPH, RDN, FACSM, FAAP ; Natalie D. Muth, MD, MPH, RDN, FACSM, FAAP. This Site. Google Scholar. Mary Tanaka, MD, MS, FAAP Mary Tanaka, MD, MS, FAAP. American Academy of Pediatrics. Within 30 minutes post workout, 1 to 1. An example of a refuel meal would be steak, potatoes, and a side of asparagus or a protein shake with protein powder, fruit, milk, and oats. click to enlarge. Carbohydrate Loading Carbohydrate loading is a dietary practice used to enhance athletic endurance performance by supplying adequate glycogen to the muscles for stored energy. Muscular fatigue is closely tied to muscle glycogen depletion. Using the practice of carbohydrate loading to maximize these stores may enable an individual to perform at a higher submaximal intensity longer before reaching muscular exhaustion. Carb loading can improve athletic performance in sports such as marathons, triathlons, ultramarathons, ultraendurance events, Nordic skiing, and long-distance swimming or cycling. In addition, it has been suggested that mid- to late-game performance in intermittent high-intensity sports, such as soccer and football, might be improved by glycogen loading, specifically when starting levels are low. Whole grains, fruits, and starchy vegetables are ways to meet this goal. A glycogen-loading meal may include baked chicken, a baked potato, one whole wheat dinner roll, roasted vegetables, a glass of milk, and a side of fruit salad. Two studies assessed the impact of dietary changes on athletic performance. In the first study, hockey players were split into two groups, one given a high-carb meal and the other a normal mixed food meal. The high-carb group showed improvement in speed, distance, and time skating compared with the control group. The second study focused on mountain bikers. The study found that the lower-carb group was faster for the first lap of the race, but by lap four all high-carbohydrate racers were ahead of the control group. These studies showed improved performance in endurance athletes who invest in carbohydrate loading before their event. Educating patients on the difference between high-quality carbohydrates and refined carbohydrates can be helpful in dispelling any food fears or myths. White believes in the power of health and fitness and has founded a nonprofit organization, the LIFT Fitness Foundation, which focuses on creating a core of wellness to empower individuals in need. References 1. Clark N. A low-carb diet for athletes? Separating fact from fiction. American Fitness website. Published Accessed April 2, Hawley JA, Leckey JJ. |
| Carbohydrates — The Top-Tier Macronutrient for Sports Performance - Today's Dietitian Magazine | Athletes need to consume enough protein to support muscle protein synthesis and prevent muscle breakdown. A balanced intake of protein throughout the day, especially after exercise, helps promote muscle recovery and adaptation. Optimal Body Composition: The right macronutrient balance can help athletes achieve and maintain a healthy body composition. Carbohydrates and proteins provide the necessary energy for training and muscle development, while fats play a role in hormone regulation and satiety. Balancing these macronutrients can support the maintenance of lean muscle mass and minimize excess body fat. Improved Immune Function: Intense exercise can temporarily weaken the immune system, making athletes more susceptible to illness and infections. A well-balanced diet, including adequate macronutrients, vitamins, and minerals, supports immune function and helps prevent illness, allowing athletes to stay consistent with their training. Faster Recovery: Proper macronutrient balance can speed up the recovery process and reduce muscle soreness after intense workouts. Consuming an appropriate combination of carbohydrates and proteins immediately after exercise helps replenish glycogen stores and promotes muscle repair and growth. Can intermittent fasting be compatible with an athletic lifestyle? Is it possible to gain weight while focusing on muscle building? Leave a Comment Cancel Reply Your email address will not be published. Popular Fitpaa Packs. Experience the best of Fitpaa services with these packs. At Fitpaa, we are on a mission to prevent premature deaths due to lifestyle diseases. It is this purpose that inspires and motivates us to do our best work every day. Contact Us. club CIE, Vindhya C4, IIIT Hyderabad, Gachibowli, Hyderabad. Working Hours. Monday to Saturday AM - PM. 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. Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Kerksick CM, Leutholtz B. Nutrient administration and resistance training. Burk A, Timpmann S, Medijainen L, Vahi M, Oopik V. Time-divided ingestion pattern of casein-based protein supplement stimulates an increase in fat-free body mass during resistance training in young untrained men. Nutr Res. Schoenfeld BJ, Aragon A, Wilborn C, Urbina SL, Hayward SE, Krieger J. Pre- versus post-exercise protein intake has similar effects on muscular adaptations. Aragon AA, Schoenfeld BJ. Nutrient timing revisited: is there a post-exercise anabolic window? Bosse JD, Dixon BM. Dietary protein to maximize resistance training: a review and examination of protein spread and change theories. Macnaughton LS, Wardle SL, Witard OC, Mcglory C, Hamilton DL, Jeromson S, et al. The response of muscle protein synthesis following whole-body resistance exercise is greater following 40 g than 20 g of ingested whey protein. Physiol Rep. Tang JE, Moore DR, Kujbida GW, Tarnopolsky MA, Phillips SM. Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. J App Physiol Bethesda, Md: West DW, Burd NA, Coffey VG, Baker SK, Burke LM, Hawley JA, et al. Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise. Geneva: World Health Organization; Series Editor : Who technical report series. Google Scholar. Joy JM, Lowery RP, Wilson JM, Purpura M, De Souza EO, Wilson SM, et al. The effects of 8 weeks of whey or rice protein supplementation on body composition and exercise performance. Bos C, Metges CC, Gaudichon C, Petzke KJ, Pueyo ME, Morens C, et al. Postprandial kinetics of dietary amino acids are the main determinant of their metabolism after soy or milk protein ingestion in humans. Burd NA, Yang Y, Moore DR, Tang JE, Tarnopolsky MA, Phillips SM. Greater stimulation of myofibrillar protein synthesis with ingestion of whey protein isolate v. Micellar casein at rest and after resistance exercise in elderly men. Br J Nutr. Phillips SM, Tang JE, Moore DR. The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons. J Am Coll Nutr. Hartman JW, Tang JE, Wilkinson SB, Tarnopolsky MA, Lawrence RL, Fullerton AV, et al. Consumption of fat-free fluid milk after resistance exercise promotes greater lean mass accretion than does consumption of soy or carbohydrate in young, novice, male weightlifters. Wilkinson SB, Tarnopolsky MA, Macdonald MJ, Macdonald JR, Armstrong D, Phillips SM. Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage. Kerksick CM, Rasmussen C, Lancaster S, Starks M, Smith P, Melton C, et al. Impact of differing protein sources and a creatine containing nutritional formula after 12 weeks of resistance training. Paddon-Jones D, Sheffield-Moore M, Aarsland A, Wolfe RR, Ferrando AA. Exogenous amino acids stimulate human muscle anabolism without interfering with the response to mixed meal ingestion. Paddon-Jones D, Sheffield-Moore M, Urban RJ, Sanford AP, Aarsland A, Wolfe RR, et al. Essential amino acid and carbohydrate supplementation ameliorates muscle protein loss in humans during 28 days bedrest. J Clin Endocrinol Metab. Phillips SM, Tipton KD, Aarsland A, Wolf SE, Wolfe RR. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Rennie MJ, Bohe J, Wolfe RR. Latency, duration and dose response relationships of amino acid effects on human muscle protein synthesis. Svanberg E, Jefferson LS, Lundholm K, Kimball SR. Postprandial stimulation of muscle protein synthesis is independent of changes in insulin. Trommelen J, Groen BB, Hamer HM, De Groot LC, Van Loon LJ. Mechanisms in endocrinology: exogenous insulin does not increase muscle protein synthesis rate when administered systemically: a systematic review. Eur J Endocrinol. Abdulla H, Smith K, Atherton PJ, Idris I. Role of insulin in the regulation of human skeletal muscle protein synthesis and breakdown: a systematic review and meta-analysis. Greenhaff PL, Karagounis LG, Peirce N, Simpson EJ, Hazell M, Layfield R, et al. Disassociation between the effects of amino acids and insulin on signaling, ubiquitin ligases, and protein turnover in human muscle. Rennie MJ, Bohe J, Smith K, Wackerhage H, Greenhaff P. Branched-chain amino acids as fuels and anabolic signals in human muscle. Power O, Hallihan A, Jakeman P. Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Staples AW, Burd NA, West DW, Currie KD, Atherton PJ, Moore DR, et al. Carbohydrate does not augment exercise-induced protein accretion versus protein alone. Baron KG, Reid KJ, Kern AS, Zee PC. Role of sleep timing in caloric intake and bmi. Obesity Silver Spring. Article Google Scholar. Ormsbee MJ, Gorman KA, Miller EA, Baur DA, Eckel LA, Contreras RJ, et al. Nighttime feeding likely alters morning metabolism but not exercise performance in female athletes. Zwaan M, Burgard MA, Schenck CH, Mitchell JE. Night time eating: a review of the literature. Eur Eat Disord Rev. Kinsey AW, Ormsbee MJ. The health impact of nighttime eating: old and new perspectives. Trommelen J, Van Loon LJ. Pre-sleep protein ingestion to improve the skeletal muscle adaptive response to exercise training. Res PT, Groen B, Pennings B, Beelen M, Wallis GA, Gijsen AP, et al. Protein ingestion before sleep improves postexercise overnight recovery. Groen BB, Res PT, Pennings B, Hertle E, Senden JM, Saris WH, et al. Intragastric protein administration stimulates overnight muscle protein synthesis in elderly men. Madzima TA, Panton LB, Fretti SK, Kinsey AW, Ormsbee MJ. Night-time consumption of protein or carbohydrate results in increased morning resting energy expenditure in active college-aged men. Kinsey AW, Eddy WR, Madzima TA, Panton LB, Arciero PJ, Kim JS, et al. Influence of night-time protein and carbohydrate intake on appetite and cardiometabolic risk in sedentary overweight and obese women. Kinsey AW, Cappadona SR, Panton LB, Allman BR, Contreras RJ, Hickner RC, et al. The effect of casein protein prior to sleep on fat metabolism in obese men. Ormsbee MJ, Kinsey AW, Eddy WR, Madzima TA, Arciero PJ, Figueroa A, et al. The influence of nighttime feeding of carbohydrate or protein combined with exercise training on appetite and cardiometabolic risk in young obese women. Figueroa A, Wong A, Kinsey A, Kalfon R, Eddy W, Ormsbee MJ. Effects of milk proteins and combined exercise training on aortic hemodynamics and arterial stiffness in young obese women with high blood pressure. Am J Hypertens. Dirks ML, Groen BB, Franssen R, Van Kranenburg J, Van Loon LJ. Neuromuscular electrical stimulation prior to presleep protein feeding stimulates the use of protein-derived amino acids for overnight muscle protein synthesis. Holwerda AM, Kouw IW, Trommelen J, Halson SL, Wodzig WK, Verdijk LB, et al. Physical activity performed in the evening increases the overnight muscle protein synthetic response to presleep protein ingestion in older men. Trommelen J, Holwerda AM, Kouw IW, Langer H, Halson SL, Rollo I, et al. Resistance exercise augments postprandial overnight muscle protein synthesis rates. Snijders T, Res PT, Smeets JS, Van Vliet S, Van Kranenburg J, Maase K, et al. Protein ingestion before sleep increases muscle mass and strength gains during prolonged resistance-type exercise training in healthy young men. Antonio J, Ellerbroek A, Peacock C, Silver T. Casein protein supplementation in trained men and women: morning versus evening. Int J Exerc Sci. Buckner SL, Leonneke JP, Loprinzi PD. Protein timing during the day and its relevance for muscle strength and lean mass. Clin Physiol Funct Imaging. doi: Mitchell CJ, Churchward-Venne TA, Parise G, Bellamy L, Baker SK, Smith K, et al. Acute post-exercise myofibrillar protein synthesis is not correlated with resistance training-induced muscle hypertrophy in young men. PLoS One. Areta JL, Burke LM, Ross ML, Camera DM, West DW, Broad EM, et al. Timing and distribution of protein ingestion during prolonged recovery from resistance exercise alters myofibrillar protein synthesis. Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, et al. Protein feeding pattern does not affect protein retention in young women. Tinsley GM, Forsse JS, Butler NK, Paoli A, Bane AA, La Bounty PM, et al. Time-restricted feeding in young men performing resistance training: a randomized controlled trial. Eur J Sport Sci. Tarnopolsky MA, Macdougall JD, Atkinson SA. Influence of protein intake and training status on nitrogen balance and lean body mass. Phillips SM, Atkinson SA, Tarnopolsky MA, Macdougall JD. Gender differences in leucine kinetics and nitrogen balance in endurance athletes. Lemon PW. Effect of exercise on protein requirements. Protein requirements and supplementation in strength sports. Tarnopolsky MA, Atkinson SA, Macdougall JD, Chesley A, Phillips S, Schwarcz HP. Evaluation of protein requirements for trained strength athletes. A brief review of higher dietary protein diets in weight loss: a focus on athletes. Witard OC, Jackman SR, Breen L, Smith K, Selby A, Tipton KD. Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise. Yang Y, Breen L, Burd NA, Hector AJ, Churchward-Venne TA, Josse AR, et al. Resistance exercise enhances myofibrillar protein synthesis with graded intakes of whey protein in older men. Bohe J, Low JF, Wolfe RR, Rennie MJ. Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. Atherton PJ, Etheridge T, Watt PW, Wilkinson D, Selby A, Rankin D, et al. Muscle full effect after oral protein: time-dependent concordance and discordance between human muscle protein synthesis and mtorc1 signaling. Wilson GJ, Layman DK, Moulton CJ, Norton LE, Anthony TG, Proud CG, et al. Leucine or carbohydrate supplementation reduces AMPK and eef2 phosphorylation and extends postprandial muscle protein synthesis in rats. Kim IY, Schutzler S, Schrader A, Spencer HJ, Azhar G, Ferrando AA, et al. The anabolic response to a meal containing different amounts of protein is not limited by the maximal stimulation of protein synthesis in healthy young adults. Arciero PJ, Ormsbee MJ, Gentile CL, Nindl BC, Brestoff JR, Ruby M. Increased protein intake and meal frequency reduces abdominal fat during energy balance and energy deficit. Ruby M, Repka CP, Arciero PJ. J Phys Act Health. Arciero PJ, Ives SJ, Norton C, Escudero D, Minicucci O, O'brien G, et al. Protein-pacing and multi-component exercise training improves physical performance outcomes in exercise-trained women: the PRISE 3 study. Ives SJ, Norton C, Miller V, Minicucci O, Robinson J, O'brien G, et al. Multi-modal exercise training and protein-pacing enhances physical performance adaptations independent of growth hormone and bdnf but may be dependent on igf-1 in exercise-trained men. Growth Hormon IGF Res. Arciero PJ, Baur D, Connelly S, Ormsbee MJ. Timed-daily ingestion of whey protein and exercise training reduces visceral adipose tissue mass and improves insulin resistance: the PRISE study. Beyond the zone: protein needs of active individuals. Campbell WW, Barton ML Jr, Cyr-Campbell D, Davey SL, Beard JL, Parise G, et al. Effects of an omnivorous diet compared with a lactoovovegetarian diet on resistance-training-induced changes in body composition and skeletal muscle in older men. Katsanos CS, Chinkes DL, Paddon-Jones D, Zhang XJ, Aarsland A, Wolfe RR. Whey protein ingestion in elderly persons results in greater muscle protein accrual than ingestion of its constituent essential amino acid content. Cuthbertson D, Smith K, Babraj J, Leese G, Waddell T, Atherton P, et al. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. Norton LE, Layman DK. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. Blomstrand E. A role for branched-chain amino acids in reducing central fatigue. Davis JM. Carbohydrates, branched-chain amino acids, and endurance: the central fatigue hypothesis. Int J Sport Nutr. Newsholme EA, Blomstrand E. Branched-chain amino acids and central fatigue. Brosnan JT, Brosnan ME. Branched-chain amino acids: enzyme and substrate regulation. Stoll B, Burrin DG. Measuring splanchnic amino acid metabolism in vivo using stable isotopic tracers. J Anim Sci. Norton L, Wilson GJ. Optimal protein intake to maximize muscle protein synthesis. AgroFood Industry Hi-Tech. Glynn EL, Fry CS, Drummond MJ, Timmerman KL, Dhanani S, Volpi E, et al. Excess leucine intake enhances muscle anabolic signaling but not net protein anabolism in young men and women. Norton LE, Layman DK, Bunpo P, Anthony TG, Brana DV, Garlick PJ. The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats. Pasiakos SM, Mcclung HL, Mcclung JP, Margolis LM, Andersen NE, Cloutier GJ, et al. Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis. Churchward-Venne TA, Burd NA, Mitchell CJ, West DW, Philp A, Marcotte GR, et al. Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance exercise in men. Layman DK. Role of leucine in protein metabolism during exercise and recovery. Cockburn E, Stevenson E, Hayes PR, Robson-Ansley P, Howatson G. Effect of milk-based carbohydrate-protein supplement timing on the attenuation of exercise-induced muscle damage. Wojcik JR, Walber-Rankin J, Smith LL, Gwazdauskas FC. Comparison of carbohydrate and milk-based beverages on muscle damage and glycogen following exercise. Watson P, Love TD, Maughan RJ, Shirreffs SM. A comparison of the effects of milk and a carbohydrate-electrolyte drink on the restoration of fluid balance and exercise capacity in a hot, humid environment. Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci. Dangin M, Boirie Y, Guillet C, Beaufrere B. Influence of the protein digestion rate on protein turnover in young and elderly subjects. Dangin M, Guillet C, Garcia-Rodenas C, Gachon P, Bouteloup-Demange C, Reiffers-Magnani K, et al. The rate of protein digestion affects protein gain differently during aging in humans. Wilson J, Wilson GJ. Contemporary issues in protein requirements and consumption for resistance trained athletes. Nair KS. Muscle protein turnover: methodological issues and the effect of aging. J Gerontol A Biol Sci Med Sci. Cribb PJ, Williams AD, Carey MF, Hayes A. The effect of whey isolate and resistance training on strength, body composition, and plasma glutamine. Morifuji M, Sakai K, Sanbongi C, Sugiura K. Dietary whey protein increases liver and skeletal muscle glycogen levels in exercise-trained rats. Markus CR, Olivier B, De Haan EH. Whey protein rich in alpha-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. Minet-Ringuet J, Le Ruyet PM, Tome D, Even PC. A tryptophan-rich protein diet efficiently restores sleep after food deprivation in the rat. Behav Brain Res. Law BA, Reiter B. The isolation and bacteriostatic properties of lactoferrin from bovine milk whey. J Dairy Res. Wang X, Ai T, Meng XL, Zhou J, Mao XY. In vitro iron absorption of alpha-lactalbumin hydrolysate-iron and beta-lactoglobulin hydrolysate-iron complexes. J Dairy Sci. Hu FB, Stampfer MJ, Rimm EB, Manson JE, Ascherio A, Colditz GA, et al. A prospective study of egg consumption and risk of cardiovascular disease in men and women. Hasler CM. The changing face of functional foods. Safety assessment and potential health benefits of food components based on selected scientific criteria. ILSI North America technical committee on food components for health promotion. Crit Rev Food Sci Nutr. Position of the American Dietetic Association. Functional foods. Blusztajn JK. Choline, a vital amine. Handelman GJ, Nightingale ZD, Lichtenstein AH, Schaefer EJ, Blumberg JB. Lutein and zeaxanthin concentrations in plasma after dietary supplementation with egg yolk. Symons TB, Schutzler SE, Cocke TL, Chinkes DL, Wolfe RR, Paddon-Jones D. Aging does not impair the anabolic response to a protein-rich meal. Fogelholm M. Dairy products, meat and sports performance. Kreider RB, Wilborn CD, Taylor L, Campbell B, Almada AL, Collins R, et al. Harris RC, Lowe JA, Warnes K, Orme CE. The concentration of creatine in meat, offal and commercial dog food. Res Vet Sci. Shomrat A, Weinstein Y, Katz A. Effect of creatine feeding on maximal exercise performance in vegetarians. Especially in the fitness realm, protein is touted as the king of macronutrients. Low-carb diets have infiltrated sports nutrition, boasting the benefits of boosted energy and increased athletic performance. The ketogenic diet is the most prevalent of the low-carb diets today. Some athletes seek to burn more fat during activity to improve performance; however, most studies show no benefit to ketosis during activity. Fat compared with carbohydrates requires more oxygen to produce energy. This means low-carb athletes would have to work at a higher level to uptake more oxygen to produce comparable energy levels as those achieved with a higher-carbohydrate diet. This means a lb male athlete would need anywhere from to g carbohydrates per day. Benefits Adequate carbohydrate intake can prevent muscle breakdown from glycogen depletion and prevent hypoglycemia, both of which have been independently proven to reduce athletic performance. Once this happens, the body needs alternative fuel sources and will turn to protein and fat in a process called gluconeogenesis. Having enough glycogen on board before exercise and refueling during workouts can help preserve skeletal muscle integrity during exercise. And as exercise intensity is increased, glycogen becomes progressively more important as a fuel source. During strenuous exercise, muscle tissue damage occurs and can continue after exercise. Due to the anabolic nature of insulin, it increases muscle amino acid uptake and protein synthesis while decreasing protein degradation. After exercise, raising the plasma insulin level within one hour is key for limiting muscle damage. They can enhance muscle glycogen storage significantly by adding protein to a carbohydrate supplement. This reduces the amount of carbohydrate required to maximize glycogen storage. If athletes consume both a protein and carbohydrate supplement post workout, they should consume 0. Downside to Low-Carb Diets Though growing in popularity, long-term low-carbohydrate diets are deemed potentially harmful to athletic performance. Research suggests that low-carb diets can lead to a decline in cognitive performance and mood, perceptions of fatigue, and lack of focus. Other data suggest a stronger risk of skeletal muscle damage during training or competing in individuals following a low-carb diet. Due to increased reliance on carbohydrates for energy during dehydration and decreased exercise economy from a low-carb diet, researchers are clear that low-carb diets make it difficult to sustain the intensity levels required for competitive and serious athletic performance. Fueling and Refueling To ensure proper muscle energy stores for sports performance, fueling and refueling before, after, and sometimes during a workout is imperative. Examples of balanced preworkout fuel are egg whites with breakfast potatoes and strawberries, Greek yogurt with berries and granola, or an apple with almond butter and a serving of whole grain crackers. Within 30 minutes post workout, 1 to 1. An example of a refuel meal would be steak, potatoes, and a side of asparagus or a protein shake with protein powder, fruit, milk, and oats. click to enlarge. |
Macronutrient Optimization for Sports and Athletic Performance -
Nutrients such as carbohydrates maintain blood glucose levels, fuel activity, and replenish energy stores while proteins aid in muscle growth, recovery, and repair muscle damage Alexander, Hydration is also critical in optimizing fluid levels, replenishing electrolytes, and preventing dehydration Callahan, Regardless of whether you are an Olympic athlete or just someone who enjoys working out at the gym, you can use appropriate nutrition and exercise to enhance your personal health and overall well-being.
Athletes have different nutritional needs compared to the general public. Not only do they require more calories to compete at their optimum level, but they also require greater amounts of macronutrients to maintain strength, endurance, and peak recovery Streit, They are used in large amounts and are essential for growth, development, and function.
All three macronutrients are involved in energy production, in addition to other key roles. You can find a breakdown of the recommended macronutrient amounts for different age groups on the Health Canada page. The following is the macronutrient breakdown for individuals aged 19 and over:. This breakdown is a recommendation and may not be appropriate for everyone.
Tweak it to suit your age, activity level, specific health needs, medical conditions, and health goals Streit, ; Health Canada, Micronutrients are vitamins and minerals which are derived largely from your diet.
While they are needed in smaller amounts than macronutrients, they play a vital role in maintaining optimal health, preventing disease, and ensuring proper body functioning. Examples of some micronutrients include vitamins A, B, C, D, E and minerals such as iron, calcium, magnesium etc.
Micronutrient Facts, Nutritional requirements also vary based on the type of sports athletes engage in Beck et al. For example, strength athletes such as powerlifters have higher protein requirements to develop lean muscle mass unlike endurance athletes marathon runners and cyclists who require greater amounts of carbohydrates to fuel themselves for hours of activity Macronutrient Needs of Endurance and Power Athletes, A more comprehensive and thorough comparison of various sports is beyond the scope of this article.
Whether you are an amateur or professional athlete, or somebody who casually enjoys an active lifestyle, considering the following will help promote your overall health and well-being.
The recommended daily caloric intake is calories a day for the average woman and calories per day for the average man. It is important to note that these numbers serve as a guide and the amount of energy you need will vary depending on your gender, height, weight, activity level, and age.
Additionally, caloric intake is not just about quantity but quality as well because the foods you eat affect your body in different ways Osilla, Athletes require a well-balanced, nutrient-rich diet with sufficient carbohydrates, proteins, healthy fats, vitamins, and minerals.
These nutrients are the foundation of general health and can help boost peak performance and recovery. Fueling and hydrating your body before, during and after workout not only affects training and performance but general comfort as well.
That said, the timing and amount of food tolerated has been found to vary among individuals. Some people report digestive struggles, such as nausea and cramping, if they consume foods too close to the start of training while others rely on it to ensure adequate blood sugar levels and top up body stores.
During a workout, you quickly lose fluid when you sweat; this fluid is a combination of water and electrolytes which if left unreplenished may cause dehydration.
Water is the best way to rehydrate. A general rule of thumb is to exercise when adequately hydrated and to drink every 15 to 20 minutes during a workout Callahan, The bottom-line is: Speak to your coach, trainer, dietitian, or doctor.
Find a nutritional strategy that works for you. Pack healthy snacks and plan ahead. Good nutrition is flexible. And it is okay to tailor it to your personal preferences, health needs and lifestyle provided you have adequate nutrition and fluid through your work-out sessions.
Most athletes fuel up with healthy carbohydrates hours before a training session while avoiding fats and proteins because they are slower to digest.
Depending on the gap between your last meal and workout sessions and the presence of distracting hunger pangs you may want to consider having a small snack such as low-fat yogurt, raisins, or a banana. After working out, eat a meal with proteins and carbohydrates to help your muscles recover and replenish your energy stores Food as Fuel Before, During and After Workouts, Here are some foods that you can consider:.
Avoid foods that are difficult to digest such as those rich in fibre or fat. Examples include dairy, beans, cruciferous vegetables broccoli, cabbage , etc.
These foods tend to remain in the stomach longer, diverting oxygen-rich blood from muscles to the stomach to aid in digestion. 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.
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.
June Issue. Isotonic sports nutrition the Macronhtrient, carbs have waxed and waned Macronutrient Optimization for Sports and Athletic Performance their favorability within the diet. In the s, Atthletic were recognized as important Otimization for athletes, while only 12 years later the Atkins diet was born and carbohydrates were demonized. In the s, carb-loading was birthed into the sports world as athletes wanted to boost energy before events. Fad Diets Currently, not much has changed in the hysteria and confusion surrounding carbohydrates. Many sports dietitians Pefformance themselves working Macronutrient Optimization for Sports and Athletic Performance an array of different sports and advising athletes with fo wide variety of needs. Endurance athletes rely on the aerobic system, while anr athletes primarily Athleitc the Personalized weight maintenance plan system the fastest way for Citrus bioflavonoids and arthritis relief body to Optimizatuon ATP. Another major difference between these two groups of athletes is the amount of energy they expend. Regardless of gender, age, or sport, endurance athletes burn a significant amount of calories during continuous distance training sessions that may last four hours and more. For them, keeping calorie intake high day after day is necessary. Power athletes, on the other hand, typically have lower calorie that may vary based on gender, age, sport, and goals. Still, sufficient calories are crucial for power athletes in preventing muscle tissue breakdown for use as energy.
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