Chocolate Protein Blend

$39.99

$39.99

Keywords: Muscle Mass, Amino Acids, Whey, Casein, Egg Albumin

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Description

Keywords: Muscle Mass, Amino Acids, Whey, Casein, Egg Albumin

Muscle is a very important metabolic tissue with a continuous turnover (1, 2). One’s muscle mass is the net balance between muscle protein synthesis and muscle breakdown (3). For a net gain of muscle mass, adequate amino acids through diet or protein supplements must be present. Muscle protein synthesis is compounded by exercise (3-5). Casein and whey, the most popular protein supplements are both dairy-sourced proteins. Whey digest relatively quickly, while casein travels slowly in the stomach and digests gradually (6-8). Casein also has less branched chain amino acids (BCAAs) than whey (9). BCAAs speed up the bioavailability of amino acids (10). The slow digestion of casein results in longer bioavailability of amino acids than whey (6, 11, 12).

There have been different research findings between casein and whey as to which offer the best muscle protein synthesis (6, 12-14). While some studies have shown no difference in muscle protein net balance between whey and casein even though the plasma amino acid profile were different (13), others demonstrated that whey provides more muscle synthesis than casein (14), yet some have shown that casein provides an overall enhanced muscle accretion than whey (6, 12). Since the science is not completely clear as to which of these protein sources is superior, we have combined these preferred protein types; Whey Concentrate, Whey Isolate and Micellar Casein Protein, in addition to pasture-raised Chicken Egg Albumin Protein to provide a rich supply of amino acids. Egg white protein has about 9% Leucine amino acid and like Whey has a highest biological value (15, 16). About 8% of casein protein is Leucine. Essential amino acids, particularly the branched-chain amino acid Leucine is critical in stimulating muscle protein synthesis (17-19).

Micellar Casein is thought to have a much controlled gastric emptying and provides sustained bioavailable amino acids (20). Whey isolate has a high percentage of pure protein (>90%), with less fat and lactose/carbohydrate than whey concentrate (21). Whey concentrate, on the other hand, has more minerals than the isolate, with ~70-85% protein (21). The compositional difference between the Whey Isolate and the Concentrate lies in the filtration process. TET METABOLIC’s Protein Blend provides 22g protein per scoop of which 10.4g are Essential Amino Acids, 5.1g as BCAA and 11% Leucine.
It should be noted that International Society Of Sports Nutrition (ISSN) recommends that your supplemental protein is sourced from both casein and whey (22). The Recommended Daily Allowance (RDA) of protein for healthy individuals is 0.8 g/kg/day (23). However, the ISSN recommends 1.4 – 2.0 g/kg/day for exercising persons (22).

Protein digestion is an independent regulating factor of protein retention (12). Effectively digested proteins are readily absorbed (24). To this end, we have complemented our protein blend with digestive enzymes and probiotics to aid in the efficient digestion.

References

1. Bohe J, Low JF, Wolfe RR, Rennie MJ. Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. J Physiol. 2001;532(Pt 2):575-9.

2. Bennet WM, Connacher AA, Scrimgeour CM, Smith K, Rennie MJ. Increase in anterior tibialis muscle protein synthesis in healthy man during mixed amino acid infusion: studies of incorporation of [1-13C]leucine. Clin Sci (Lond). 1989;76(4):447-54.

3. Rennie MJ, Wackerhage H, Spangenburg EE, Booth FW. Control of the size of the human muscle mass. Annu Rev Physiol. 2004;66:799-828.

4. 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. Am J Physiol. 1995;268(3 Pt 1):E514-20.

5. Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB, et al. Whey and casein labeled with L-[1-13C]leucine and muscle protein synthesis: effect of resistance exercise and protein ingestion. Am J Physiol Endocrinol Metab. 2011;300(1):E231-42.

6. 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 U S A. 1997;94(26):14930-5.

7. Daniel H, Vohwinkel M, Rehner G. Effect of casein and beta-casomorphins on gastrointestinal motility in rats. J Nutr. 1990;120(3):252-7.

8. Wilson J, Wilson GJ. Contemporary issues in protein requirements and consumption for resistance trained athletes. J Int Soc Sports Nutr. 2006;3:7-27.

9. Layman DK, Baum JI. Dietary protein impact on glycemic control during weight loss. J Nutr. 2004;134(4):968S-73S.

10. Fouillet H, Mariotti F, Gaudichon C, Bos C, Tome D. Peripheral and splanchnic metabolism of dietary nitrogen are differently affected by the protein source in humans as assessed by compartmental modeling. J Nutr. 2002;132(1):125-33.

11. 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. J Nutr. 2003;133(5):1308-15.

12. Dangin M, Boirie Y, Garcia-Rodenas C, Gachon P, Fauquant J, Callier P, et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab. 2001;280(2):E340-8.

13. 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. Med Sci Sports Exerc. 2004;36(12):2073-81.

14. 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. J Physiol. 2003;549(Pt 2):635-44.

15. 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. Nutrients. 2012;4(10):1504-17.

16. Miranda JM, Anton X, Redondo-Valbuena C, Roca-Saavedra P, Rodriguez JA, Lamas A, et al. Egg and egg-derived foods: effects on human health and use as functional foods. Nutrients. 2015;7(1):706-29.

17. Breen L, Churchward-Venne TA. Leucine: a nutrient ‘trigger’ for muscle anabolism, but what more? J Physiol. 2012;590(9):2065-6.

18. Atherton PJ, Smith K, Etheridge T, Rankin D, Rennie MJ. Distinct anabolic signalling responses to amino acids in C2C12 skeletal muscle cells. Amino Acids. 2010;38(5):1533-9.

19. Volpi E, Kobayashi H, Sheffield-Moore M, Mittendorfer B, Wolfe RR. Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults. Am J Clin Nutr. 2003;78(2):250-8.

20. 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 Appl Physiol (1985). 2009;107(3):987-92.

21. Hoffman JR, Falvo MJ. Protein – Which is Best? J Sports Sci Med. 2004;3(3):118-30.

22. 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. 2007;4:8.

23. Trumbo P, Schlicker S, Yates AA, Poos M, Food, Nutrition Board of the Institute of Medicine TNA. Dietary reference intakes for energy, carbohydrate, fiber, fat, fatty acids, cholesterol, protein and amino acids. J Am Diet Assoc. 2002;102(11):1621-30.

24. Grimble GK, Rees RG, Keohane PP, Cartwright T, Desreumaux M, Silk DB. Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastroenterology. 1987;92(1):136-42.

Product Information

Keywords: Muscle Mass, Amino Acids, Whey, Casein, Egg Albumin

Supplement Fact

Product Literature

Muscle is a very important metabolic tissue with a continuous turnover (1, 2). One’s muscle mass is the net balance between muscle protein synthesis and muscle breakdown (3). For a net gain of muscle mass, adequate amino acids through diet or protein supplements must be present. Muscle protein synthesis is compounded by exercise (3-5). Casein and whey, the most popular protein supplements are both dairy-sourced proteins. Whey digest relatively quickly, while casein travels slowly in the stomach and digests gradually (6-8). Casein also has less branched chain amino acids (BCAAs) than whey (9). BCAAs speed up the bioavailability of amino acids (10). The slow digestion of casein results in longer bioavailability of amino acids than whey (6, 11, 12).

There have been different research findings between casein and whey as to which offer the best muscle protein synthesis (6, 12-14). While some studies have shown no difference in muscle protein net balance between whey and casein even though the plasma amino acid profile were different (13), others demonstrated that whey provides more muscle synthesis than casein (14), yet some have shown that casein provides an overall enhanced muscle accretion than whey (6, 12). Since the science is not completely clear as to which of these protein sources is superior, we have combined these preferred protein types; Whey Concentrate, Whey Isolate and Micellar Casein Protein, in addition to pasture-raised Chicken Egg Albumin Protein to provide a rich supply of amino acids. Egg white protein has about 9% Leucine amino acid and like Whey has a highest biological value (15, 16). About 8% of casein protein is Leucine. Essential amino acids, particularly the branched-chain amino acid Leucine is critical in stimulating muscle protein synthesis (17-19).

Micellar Casein is thought to have a much controlled gastric emptying and provides sustained bioavailable amino acids (20). Whey isolate has a high percentage of pure protein (>90%), with less fat and lactose/carbohydrate than whey concentrate (21). Whey concentrate, on the other hand, has more minerals than the isolate, with ~70-85% protein (21). The compositional difference between the Whey Isolate and the Concentrate lies in the filtration process. TET METABOLIC’s Protein Blend provides 22g protein per scoop of which 10.4g are Essential Amino Acids, 5.1g as BCAA and 11% Leucine.
It should be noted that International Society Of Sports Nutrition (ISSN) recommends that your supplemental protein is sourced from both casein and whey (22). The Recommended Daily Allowance (RDA) of protein for healthy individuals is 0.8 g/kg/day (23). However, the ISSN recommends 1.4 – 2.0 g/kg/day for exercising persons (22).

Protein digestion is an independent regulating factor of protein retention (12). Effectively digested proteins are readily absorbed (24). To this end, we have complemented our protein blend with digestive enzymes and probiotics to aid in the efficient digestion.

References
1. Bohe J, Low JF, Wolfe RR, Rennie MJ. Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. J Physiol. 2001;532(Pt 2):575-9.

2. Bennet WM, Connacher AA, Scrimgeour CM, Smith K, Rennie MJ. Increase in anterior tibialis muscle protein synthesis in healthy man during mixed amino acid infusion: studies of incorporation of [1-13C]leucine. Clin Sci (Lond). 1989;76(4):447-54.

3. Rennie MJ, Wackerhage H, Spangenburg EE, Booth FW. Control of the size of the human muscle mass. Annu Rev Physiol. 2004;66:799-828.

4. 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. Am J Physiol. 1995;268(3 Pt 1):E514-20.

5. Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB, et al. Whey and casein labeled with L-[1-13C]leucine and muscle protein synthesis: effect of resistance exercise and protein ingestion. Am J Physiol Endocrinol Metab. 2011;300(1):E231-42.

6. 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 U S A. 1997;94(26):14930-5.

7. Daniel H, Vohwinkel M, Rehner G. Effect of casein and beta-casomorphins on gastrointestinal motility in rats. J Nutr. 1990;120(3):252-7.

8. Wilson J, Wilson GJ. Contemporary issues in protein requirements and consumption for resistance trained athletes. J Int Soc Sports Nutr. 2006;3:7-27.

9. Layman DK, Baum JI. Dietary protein impact on glycemic control during weight loss. J Nutr. 2004;134(4):968S-73S.

10. Fouillet H, Mariotti F, Gaudichon C, Bos C, Tome D. Peripheral and splanchnic metabolism of dietary nitrogen are differently affected by the protein source in humans as assessed by compartmental modeling. J Nutr. 2002;132(1):125-33.

11. 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. J Nutr. 2003;133(5):1308-15.

12. Dangin M, Boirie Y, Garcia-Rodenas C, Gachon P, Fauquant J, Callier P, et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab. 2001;280(2):E340-8.

13. 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. Med Sci Sports Exerc. 2004;36(12):2073-81.

14. 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. J Physiol. 2003;549(Pt 2):635-44.

15. 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. Nutrients. 2012;4(10):1504-17.

16. Miranda JM, Anton X, Redondo-Valbuena C, Roca-Saavedra P, Rodriguez JA, Lamas A, et al. Egg and egg-derived foods: effects on human health and use as functional foods. Nutrients. 2015;7(1):706-29.

17. Breen L, Churchward-Venne TA. Leucine: a nutrient ‘trigger’ for muscle anabolism, but what more? J Physiol. 2012;590(9):2065-6.

18. Atherton PJ, Smith K, Etheridge T, Rankin D, Rennie MJ. Distinct anabolic signalling responses to amino acids in C2C12 skeletal muscle cells. Amino Acids. 2010;38(5):1533-9.

19. Volpi E, Kobayashi H, Sheffield-Moore M, Mittendorfer B, Wolfe RR. Essential amino acids are primarily responsible for the amino acid stimulation of muscle protein anabolism in healthy elderly adults. Am J Clin Nutr. 2003;78(2):250-8.

20. 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 Appl Physiol (1985). 2009;107(3):987-92.

21. Hoffman JR, Falvo MJ. Protein – Which is Best? J Sports Sci Med. 2004;3(3):118-30.

22. 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. 2007;4:8.

23. Trumbo P, Schlicker S, Yates AA, Poos M, Food, Nutrition Board of the Institute of Medicine TNA. Dietary reference intakes for energy, carbohydrate, fiber, fat, fatty acids, cholesterol, protein and amino acids. J Am Diet Assoc. 2002;102(11):1621-30.

24. Grimble GK, Rees RG, Keohane PP, Cartwright T, Desreumaux M, Silk DB. Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastroenterology. 1987;92(1):136-42.

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