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• International society of sports nutrition
• International society for sports nutrition

International society of sports nutrition

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 sportsandcasino. 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 . Research indicates that amino acids are absorbed more rapidly when they are consumed as di and/or tri peptides compared to free form amino acids or complete proteins . Further, the rate of absorption may lead to a more favorable anabolic hormonal environment . Calbet et al. examined both amino acid appearance and insulin responses following consumption of protein solutions containing the same amount of protein, or pure carbohydrates. The treatments consisted of a pure glucose solution, whey peptide hydrolysates, and cow’s milk containing milk proteins, lactose and fat. 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 0.8 between plasma amino acids and the insulin response in the peptide hydrolysates. One of the inherent shortcomings of this study is that milk proteins are 80% casein and, therefore, are not ideal candidates to compare with hydrolyzed whey.

Hoffman JR, Ratamess NA, Kang J, Falvo MJ, Faigenbaum AD. Effects of protein supplementation on muscular performance and resting hormonal changes in college football players. J Sports Sci Med. 2007;6:85–92.

The International Society of Sports Nutrition (ISSN) provides an objective and critical review related to the intake of protein for healthy, exercising individuals. Based on the current available literature, the position of the Society is as follows:An acute exercise stimulus, particularly resistance exercise, and protein ingestion both stimulate muscle protein synthesis (MPS) and are synergistic when protein consumption occurs before or after resistance exercise.For building muscle mass and for maintaining muscle mass through a positive muscle protein balance, an overall daily protein intake in the range of 1.4-2.0 g protein/kg body weight/day (g/kg/d) is sufficient for most exercising individuals, a value that falls in line within the Acceptable Macronutrient Distribution Range published by the Institute of Medicine for protein.Higher protein intakes (2.3-3.1 g/kg/d) may be needed to maximize the retention of lean body mass in resistance-trained subjects during hypocaloric periods.There is novel evidence that suggests higher protein intakes (>3.0 g/kg/d) may have positive effects on body composition in resistance-trained individuals (i.e., promote loss of fat mass).Recommendations regarding the optimal protein intake per serving for athletes to maximize MPS are mixed and are dependent upon age and recent resistance exercise stimuli. General recommendations are 0.25 g of a high-quality protein per kg of body weight, or an absolute dose of 20-40 g.Acute protein doses should strive to contain 700-3000 mg of leucine and/or a higher relative leucine content, in addition to a balanced array of the essential amino acids (EAAs).These protein doses should ideally be evenly distributed, every 3-4 h, across the day.The optimal time period during which to ingest protein is likely a matter of individual tolerance, since benefits are derived from pre- or post-workout ingestion; however, the anabolic effect of exercise is long-lasting (at least 24 h), but likely diminishes with increasing time post-exercise.While it is possible for physically active individuals to obtain their daily protein requirements through the consumption of whole foods, supplementation is a practical way of ensuring intake of adequate protein quality and quantity, while minimizing caloric intake, particularly for athletes who typically complete high volumes of training. Rapidly digested proteins that contain high proportions of essential amino acids (EAAs) and adequate leucine, are most effective in stimulating MPS. Different types and quality of protein can affect amino acid bioavailability following protein supplementation. Athletes should consider focusing on whole food sources of protein that contain all of the EAAs (i.e., it is the EAAs that are required to stimulate MPS). Endurance athletes should focus on achieving adequate carbohydrate intake to promote optimal performance; the addition of protein may help to offset muscle damage and promote recovery. Pre-sleep casein protein intake (30-40 g) provides increases in overnight MPS and metabolic rate without influencing lipolysis.

International society of sports nutrition

Recent studies in rodents indicate that a combination of exercise training and supplementation with nicotinamide adenine dinucleotide (NAD+) precursors has synergistic effects. However, there are currently no hum…

Tart cherry supplementation has been shown to enhance recovery from strenuous exercise due to its antioxidant properties. The majority of these studies used tart cherry juice, with a significant calorie conten…

This study aimed to investigate the effect of multi-ingredient intra- (BA) versus extra- (ALK) cellular buffering factor supplementation, combined with the customary intake of branched-chain amino acids (BCAA)…

Exercise increases skeletal muscle reactive oxygen species (ROS) production, which may contribute to the onset of muscular fatigue and impair athletic performance. Mitochondria-targeted antioxidants such as Mi…

While it is possible for physically active individuals to obtain their daily protein requirements through the consumption of whole foods, supplementation is a practical way of ensuring intake of adequate protein quality and quantity, while minimizing caloric intake, particularly for athletes who typically complete high volumes of training.

Isomaltulose has been discussed as a low glycaemic carbohydrate but evidence concerning performance benefits and physiological responses has produced varying results. Therefore, we primarily aimed to investiga…

International society for sports nutrition

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. J Nutr. 2010;140:1970–6.

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. Am J Clin Nutr. 2002;75:1051–6.

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. Br J Nutr. 2012;108:1780–8.

Norton LE, Rupassara I, Garlick PJ, Layman DK. Leucine contents of isonitrogenout protein sources predict post prandial muscle protein synthesis in rats fed a complete meal. FASEB J. 2009;23(Supplement 1):227–4.

Reidy PT, Walker DK, Dickinson JM, Gundermann DM, Drummond MJ, Timmerman KL, et al. Protein blend ingestion following resistance exercise promotes human muscle protein synthesis. J Nutr. 2013;143:410–6.

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