Application of Protein or Protein Hydrolysates to Improve Postexercise Recovery

2007 ◽  
Vol 17 (s1) ◽  
pp. S104-S117 ◽  
Author(s):  
Luc J.C. van Loon

Protein, protein hydrolysates, and amino acids have become popular ingredients in sports nutrition. The use of protein, protein hydrolysates, and amino acid mixtures has multiple applications when aiming to improve post exercise recovery. After exhaustive endurance-type exercise, muscle glycogen repletion is the most important factor determining the time needed to recover. Coingestion of relatively small amounts of protein and/or amino acids with carbohydrate can be used to augment postprandial insulin secretion and accelerate muscle glycogen synthesis rates. Furthermore, it has been well established that ingesting protein, protein hydrolysates, and amino acid can stimulate protein synthesis and inhibit protein breakdown and, as such, improve net muscle protein balance after resistance- or endurance-type exercise. The latter has been suggested to lead to a more effective adaptive response to each successive exercise bout. To augment net muscle protein accretion, athletes involved in resistance-type exercise generally ingest both protein and carbohydrate during post exercise recovery. However, carbohydrate ingestion after resistance-type exercise does not seem to be warranted to further stimulate muscle protein synthesis or improve whole-body protein balance when ample protein has already been ingested. Because resistance-type exercise is also associated with a substantial reduction in muscle glycogen content, it would be preferred to coingest some carbohydrate when aiming to accelerate glycogen repletion. More research is warranted to assess the impact of ingesting different proteins, protein hydrolysates, and/or amino acids on muscle protein accretion after exercise.

Author(s):  
Milou Beelen ◽  
Louise M. Burke ◽  
Martin J. Gibala ◽  
Luc J.C. van Loon

During postexercise recovery, optimal nutritional intake is important to replenish endogenous substrate stores and to facilitate muscle-damage repair and reconditioning. After exhaustive endurance-type exercise, muscle glycogen repletion forms the most important factor determining the time needed to recover. Postexercise carbohydrate (CHO) ingestion has been well established as the most important determinant of muscle glycogen synthesis. Coingestion of protein and/or amino acids does not seem to further increase muscle glycogensynthesis rates when CHO intake exceeds 1.2 g · kg−1 · hr−1. However, from a practical point of view it is not always feasible to ingest such large amounts of CHO. The combined ingestion of a small amount of protein (0.2–0.4 g · (0.2−0.4 g · kg−1 · hr−1) with less CHO (0.8 g · kg−1 · hr−1) stimulates endogenous insulin release and results in similar muscle glycogen-repletion rates as the ingestion of 1.2 g · kg−1 · hr−1 CHO. Furthermore, postexercise protein and/or amino acid administration is warranted to stimulate muscle protein synthesis, inhibit protein breakdown, and allow net muscle protein accretion. The consumption of ~20 g intact protein, or an equivalent of ~9 g essential amino acids, has been reported to maximize muscle protein-synthesis rates during the first hours of postexercise recovery. Ingestion of such small amounts of dietary protein 5 or 6 times daily might support maximal muscle protein-synthesis rates throughout the day. Consuming CHO and protein during the early phases of recovery has been shown to positively affect subsequent exercise performance and could be of specific benefit for athletes involved in multiple training or competition sessions on the same or consecutive days.


2013 ◽  
Vol 110 (6) ◽  
pp. 981-987 ◽  
Author(s):  
Atsushi Kanda ◽  
Kyosuke Nakayama ◽  
Tomoyuki Fukasawa ◽  
Jinichiro Koga ◽  
Minoru Kanegae ◽  
...  

It is well known that ingestion of a protein source is effective in stimulating muscle protein synthesis after exercise. In addition, there are numerous reports on the impact of leucine and leucine-rich whey protein on muscle protein synthesis and mammalian target of rapamycin (mTOR) signalling. However, there is only limited information on the effects of whey protein hydrolysates (WPH) on muscle protein synthesis and mTOR signalling. The aim of the present study was to compare the effects of WPH and amino acids on muscle protein synthesis and the initiation of translation in skeletal muscle during the post-exercise phase. Male Sprague–Dawley rats swam for 2 h to depress muscle protein synthesis. Immediately after exercise, the animals were administered either carbohydrate (CHO), CHO plus an amino acid mixture (AA) or CHO plus WPH. At 1 h after exercise, the supplements containing whey-based protein (AA and WPH) caused a significant increase in the fractional rate of protein synthesis (FSR) compared with CHO. WPH also caused a significant increase in FSR compared with AA. Post-exercise ingestion of WPH caused a significant increase in the phosphorylation of mTOR levels compared with AA or CHO. In addition, WPH caused greater phosphorylation of ribosomal protein S6 kinase and eukaryotic initiation factor 4E-binding protein 1 than AA and CHO. In contrast, there was no difference in plasma amino acid levels following supplementation with either AA or WPH. These results indicate that WPH may include active components that are superior to amino acids for stimulating muscle protein synthesis and initiating translation.


2014 ◽  
Vol 39 (3) ◽  
pp. 329-339 ◽  
Author(s):  
Oliver C. Witard ◽  
Tara L. Cocke ◽  
Arny A. Ferrando ◽  
Robert R. Wolfe ◽  
Kevin D. Tipton

Relative to essential amino acids (EAAs), carbohydrate (CHO) ingestion stimulates a delayed response of net muscle protein balance (NBAL). We investigated if staggered ingestion of CHO and EAA would superimpose the response of NBAL following resistance exercise, thus resulting in maximal anabolic stimulation. Eight recreationally trained subjects completed 2 trials: combined (COMB — drink 1, CHO+EAA; drink 2, placebo) and separated (SEP — drink 1, CHO; drink 2, EAA) post-exercise ingestion of CHO and EAA. Drink 1 was administered 1 h following an acute exercise bout and was followed 1 h later by drink 2. A primed, continuous infusion of l-[ring-13C6]-phenylalanine was combined with femoral arteriovenous sampling and muscle biopsies for the determination of muscle protein kinetics. Arterial amino acid concentrations increased following ingestion of EAA in both conditions. No difference between conditions was observed for phenylalanine delivery to the leg (COMB: 167 ± 23 μmol·min−1·(100 mL leg vol)−1 × 6 h; SEP: 167 ± 21 μmol·min−1·(100 mL leg vol)−1 × 6 h, P > 0.05). In the first hour following ingestion of the drink containing EAA, phenylalanine uptake was 50% greater for the SEP trial than the COMB trial. However, phenylalanine uptake was similar for COMB (110 ± 19 mg) and SEP (117 ± 24 mg) over the 6 h period. These data suggest that whereas separation of CHO and EAA ingestion following exercise may have a transient physiological impact on NBAL, this response is not reflected over a longer period. Thus, separation of CHO and EAA ingestion is unnecessary to optimize post-exercise muscle protein metabolism.


2020 ◽  
Vol 26 ◽  
Author(s):  
Su-Fen Liao ◽  
Mallikarjuna Korivi ◽  
Jung-Piao Taso ◽  
Chun-Ching Huang ◽  
Chia-Chen Chang ◽  
...  

Background: Capsinoids (CSN), the novel non-pungent capsaicin analogs have been reported to promote metabolic health and exercise tolerance. However, the effect of CSN on fat oxidation and changes in skeletal muscle glycogen levels during post-exercise recovery has not been investigated in humans. Purpose: We examined the effect of CSN supplementation on energy reliance, glycogen resynthesis and molecular proteins in the skeletal muscle of young adults during post-exercise recovery. Methods: In this crossover-designed study, nine healthy adult male volunteers (aged 21.4±0.2 years, BMI 21.9±1.3 kg/m2 ) completed a 60-min cycling exercise at 70% VO2max. Participants consumed either CSN (12 mg, single dosage) or placebo capsules with a high-carbohydrate meal (2 g carb/kg bodyweight) immediately after exercise. Biopsied muscle samples (vastus lateralis), blood and gaseous samples were obtained during 3h post-exercise recovery period. Results: We found that oral CSN supplementation right after exercise significantly altered the energy reliance on fat oxidation during recovery. This was evidenced by lower respiratory exchange ratio (RER) and higher fat oxidation rate in CSN trial. Despite, acute CSN dosage does not contribute to enhance the glycogen replenishment in skeletal muscle during 3h recovery. We identified no significant differences in postprandial glucose and insulin area under the curve in both trials. Western blot data showed increased muscle GLUT4 expression, but no significant response of p-Akt/Akt ratio with CSN during post-exercise recovery. Conclusion: Our findings conclude that acute CSN intake could change energy reliance on fat oxidation, but unable to enhance muscle glycogen resynthesis during post-exercise recovery. Thus, ergogenic properties of CSN in relevance to muscle glycogen restoration following exercise needs to be further investigated in young adults.


2018 ◽  
Vol 15 (1) ◽  
Author(s):  
Michael Mazzulla ◽  
Kimberly A. Volterman ◽  
Jeff E. Packer ◽  
Denise J. Wooding ◽  
Jahmal C. Brooks ◽  
...  

1999 ◽  
Vol 276 (4) ◽  
pp. E628-E634 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando ◽  
Stuart M. Phillips ◽  
David Doyle ◽  
Robert R. Wolfe

We examined the response of net muscle protein synthesis to ingestion of amino acids after a bout of resistance exercise. A primed, constant infusion ofl-[ ring-2H5]phenylalanine was used to measure net muscle protein balance in three male and three female volunteers on three occasions. Subjects consumed in random order 1 liter of 1) a mixed amino acid (40 g) solution (MAA), 2) an essential amino acid (40 g) solution (EAA), and 3) a placebo solution (PLA). Arterial amino acid concentrations increased ∼150–640% above baseline during ingestion of MAA and EAA. Net muscle protein balance was significantly increased from negative during PLA ingestion (−50 ± 23 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) to positive during MAA ingestion (17 ± 13 nmol ⋅ min−1 ⋅ 100 ml leg volume−1) and EAA (29 ± 14 nmol ⋅ min−1 ⋅ 100 ml leg volume−1; P < 0.05). Because net balance was similar for MAA and EAA, it does not appear necessary to include nonessential amino acids in a formulation designed to elicit an anabolic response from muscle after exercise. We concluded that ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused.


Cryobiology ◽  
2013 ◽  
Vol 66 (3) ◽  
pp. 250-255 ◽  
Author(s):  
Dustin Slivka ◽  
Matthew Heesch ◽  
Charles Dumke ◽  
John Cuddy ◽  
Walter Hailes ◽  
...  

2006 ◽  
Vol 31 (5) ◽  
pp. 518-529 ◽  
Author(s):  
Sarah B. Wilkinson ◽  
Paul L. Kim ◽  
David Armstrong ◽  
Stuart M. Phillips

We examined the effect of a post-exercise oral carbohydrate (CHO, 1 g·kg–1·h–1) and essential amino acid (EAA, 9.25 g) solution containing glutamine (0.3 g/kg BW; GLN trial) versus an isoenergetic CHO–EAA solution without glutamine (control, CON trial) on muscle glycogen resynthesis and whole-body protein turnover following 90 min of cycling at 65% VO2 peak. Over the course of 3 h of recovery, muscle biopsies were taken to measure glycogen resynthesis and mixed muscle protein synthesis (MPS), by incorporation of [ring-2H5] phenylalanine. Infusion of [1-13C] leucine was used to measure whole-body protein turnover. Exercise resulted in a significant decrease in muscle glycogen (p < 0.05) with similar declines in each trial. Glycogen resynthesis following 3 h of recovery indicated no difference in total accumulation or rate of repletion. Leucine oxidation increased 2.5 fold (p < 0.05) during exercise, returned to resting levels immediately post-exercise,and was again elevated at 3 h post-exercise (p < 0.05). Leucine flux, an index of whole-body protein breakdown rate, was reduced during exercise, but increased to resting levels immediately post-exercise, and was further increased at 3 h post-exercise (p < 0.05), but only during the CON trial. Exercise resulted in a marked suppression of whole-body protein synthesis (50% of rest; p < 0.05), which was restored post-exercise; however, the addition of glutamine did not affect whole-body protein synthesis post-exercise. The rate of MPS was not different between trials. The addition of glutamine to a CHO + EAA beverage had no effect on post-exercise muscle glycogen resynthesis or muscle protein synthesis, but may suppress a rise in whole-body proteolysis during the later stages of recovery.


2007 ◽  
Vol 39 (Supplement) ◽  
pp. S290
Author(s):  
Wen-Chih Lee ◽  
Wei-Shiang Lin ◽  
Mei-Chih Chen ◽  
Jung-Shi Wang ◽  
Kuo-Lung Ho ◽  
...  

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