WHEY PROTEIN

Por BRUNO MOTTA

WHEY PROTEIN: COMO ESCOLHER UM BOM SUPLEMENTO?

Uma das perguntas que eu mais recebo dos meus pacientes e também de quem me acompanha nas redes sociais é:

“Bruno, como eu faço pra escolher um bom suplemento de Whey Protein?”

Por mais simples que pareça essa pergunta, na verdade – escolher um bom suplemento de Whey Protein – não é uma tarefa fácil nem mesmo para quem já está habituado a comprar, principalmente, devido a grande diversidade de produtos que existe atualmente.

Por um lado, isso é algo muito positivo, tendo em vista que essa maior variedade de marcas aumenta a concorrência, e com isso, os custos acabam ficando (um pouco) mais baixos.

Ao mesmo tempo, quanto mais possibilidades surgem, maiores são as dúvidas geradas com relação a escolha de um bom produto pelo consumidor.

As diversas opções de Whey Protein acabam se tornando um verdadeiro labirinto para quem não entende muito bem sobre algumas questões específicas relacionadas a este suplemento.

Além disso, infelizmente, muitos produtos que são comercializados não apresentam uma boa qualidade.

Essa situação fica ainda pior se considerarmos o cenário de fiscalização e o controle de qualidade desses produtos que é realizado em nosso País.

Aqui no Brasil, suplementos em pó são isentos de fiscalização.

Por incrível que pareça, o órgão responsável por esse tipo de controle (ANVISA), libera a venda do produto de acordo com o primeiro registro que é fornecido pela marca/empresa, não havendo nenhuma análise posterior ou periódica referente aos demais lotes que são comercializados.

Isso faz com que algumas marcas lancem o primeiro lote do produto com uma proteína de melhor qualidade para conseguir passar na fiscalização e apresentar essa informação no rótulo da embalagem.

Contudo, após a comercialização desses primeiros lotes, a matéria-prima inicial acaba sendo substituída por uma de menor custo, e consequentemente, de pior qualidade, sem que ocorra a alteração dessas informações na embalagem.

E como o produto já passou pela fiscalização, caso ele seja consultado no site da ANVISA, irá constar o registro da matéria prima que foi utilizada inicialmente.

É revoltante isso né? Eu sei. Imagina como eu me sinto sendo nutricionista… 

Além disso, não existe um laudo de certificação de qualidade nacional ou internacional para o Whey Protein como ocorre para a avaliação de alguns outros suplementos como o Ômega 3, por exemplo, que possui o IFOS (International Fish Oil Standards Program), um certificado que é emitido mundialmente para atestar a qualidade dos suplementos de ômega-3.

Contudo, mesmo diante desses fatos, se você prestar atenção em alguns detalhes importantes que eu vou te explicar, será totalmente possível escolher um bom suplemento de Whey Protein que atenda às suas necessidades, sem pesar muito no bolso e, sem comprometer a tua saúde.

Nós vamos conversar melhor sobre esses detalhes a partir de agora…

whey protein

“O Whey Protein é um suplemento muito versátil que pode ser consumido por pessoas que possuem diferentes objetivos e finalidades. Sendo assim, vale a pena você parar alguns minutos do seu dia e avaliar com calma as opções existentes pra fazer a melhor escolha possível de acordo com às suas reais necessidades.”

1. QUAL É O SEU OBJETIVO?

O primeiro ponto que você precisa considerar pode parecer meio óbvio, mas ele passa despercebido pela grande maioria das pessoas: qual é o seu objetivo ao consumir um suplemento como Whey Protein?

  • Ganhar massa muscular Emagrecer? 
  • Complementar sua dieta com um maior aporte proteico??
  • Algum outro motivo de saúde como tratamento de doenças e condições clínicas como a sarcopenia?

 

Sim! Todos esses objetivos são perfeitamente atendidos pela suplementação de Whey Protein, desde que você utilize um suplemento de qualidade e faça a utilização da forma adequada de acordo com o que você realmente precisa.

Ter o seu objetivo bem claro é o primeiro passo para que você consiga definir qual o melhor Whey Protein.

Por exemplo: se seu foco for emagrecimento, talvez seja mais indicado que você use um Whey Protein Isolado, tendo em vista que essa versão apresenta uma composição nutricional com mais proteínas e com menos carboidratos do que as versões concentradas.

Isso não significa que um Whey Protein Concentrado seja ruim, longe disso. Essa versão também pode ser uma boa opção, principalmente, se a porção de carboidratos contida no produto estiver calculada dentro do seu planejamento nutricional (dieta).

Já para pessoas que possuem alguma intolerância a lactose ou desconfortos gastrointestinais, existe a versão hidrolisada, que nutricionalmente, não possui praticamente nenhuma diferença do Whey Protein Isolado, mas apresenta uma melhor digestibilidade pela questão da proteína passar por um processo de quebra (hidrólise) a mais do que nas versões concentradas e isoladas.

Porém, como o preço do Whey Protein Hidrolisado é bem maior do que as versões concentradas e isoladas, essa versão, normalmente, não possui um bom custo-benefício.

Um ponto que algumas pessoas levam em consideração na hora de escolher um Whey Protein é o sabor do produto.

Contudo, na grande maioria das vezes, o Whey Protein “mais docinho” não é o que possui a melhor qualidade nutricional.

Isso acontece, porque pra melhorar o sabor do produto, as empresas adicionam ingredientes como açúcares, adoçantes artificiais, aromatizantes entre outros aditivos que não são nem um pouco interessantes para a nossa saúde.

Por isso, que mais uma vez: ter seu objetivo bem claro é essencial para você encontrar um suplemento de Whey Protein que atenda às suas necessidades.

Se o seu foco for saúde, o ideal é buscar um Whey Protein que tenha um sabor agradável, mas que ao mesmo tempo, seja o mais natural possível e isento de aditivos químicos e ingredientes de baixa qualidade na composição.

Até porque, hoje em dia é bem difícil você encontrar um Whey Protein que possua um gosto ruim, mas às vezes, ele não vai ser tão doce.

Portanto, se você quer emagrecer ou ganhar massa muscular, mas também se preocupa com a saúde, procure um Whey Protein que possua ingredientes mais naturais e menos artificiais.

2. DEFINA O TIPO DE WHEY PROTEIN

Uma das razões pelas quais escolher um Whey Protein de qualidade gera tanta dificuldade, é em função da grande variedade de versões de proteína do soro do leite existentes no mercado.

Isso porque a preocupação não é somente com a marca, mas também com o tipo de proteína que vai ser encontrada dentro do produto.

Basicamente, existem três tipos de Whey Protein:

  • Whey Protein Concentrado: é a versão mais simples, e consequentemente, mais barata. Em função disso, é a que possui a maior concentração de carboidratos e de gorduras na composição.
  • Whey Protein Isolado: é o tipo que possui o melhor custo-benefício. Como o próprio nome já sugere, a proteína do produto é mais isolada, ou seja, esse tipo de Whey Protein apresenta uma menor quantidade de carboidratos e de gorduras na composição. Devido a isso, o preço desse Whey Protein possui um valor maior do que os valores das versões concentradas.
  • Whey Protein Hidrolisado: esse tipo de Whey Protein passa por um processo de hidrólise (quebra da proteína em frações menores), tornando o suplemento ainda mais fácil de ser digerido e absorvido pelo nosso organismo. É indicado para pessoas que possuem uma maior sensibilidade gastrointestinal ou em processo de recuperação de cirurgias como a bariátrica, por exemplo. Dentre os 3 tipos de Whey Protein existentes, essa versão e a que possui o valor mais elevado.

3. OBSERVE O FORNECEDOR DA MATÉRIA-PRIMa

Talvez você já tenha ouvido falar que: “um suplemento só é bom se for importado.”

Embora essa afirmação não seja 100% verdadeira, se tratando especificamente de matéria-prima para a fabricação de Whey Protein, de fato, as melhores fabricantes são de fora do Brasil (pelo menos, por enquanto).

Exatamente por isso, que quase todas as marcas nacionais importam sua matéria-prima de fora do País. 

Pra você ter uma ideia, mais de 90% dos suplementos de Whey Protein disponíveis no mercado brasileiro são fabricados com matéria-prima importada.

Mas não se engane em achar que o nome da marca tem que ser americana ou que rótulo precisa estar em inglês para ser um bom produto, longe disso.

Até porque, algumas marcas nacionais chegam a ser melhores do que muitas marcas importadas.

Como essa informação é super positiva para os produtos de boa qualidade, marcas confiáveis gostam de divulgar quem é o seu fornecedor de matéria-prima, especialmente aquelas que realmente estão comprometidas em entregar um produto de boa qualidade.

Apesar de não existir um órgão fiscalizador específico responsável pela emissão de um laudo que ateste a qualidade do produto, todas as grandes marcas possuem um laudo técnico da matéria-prima que é utilizada.

Através desse laudo você consegue identificar se a matéria-prima utilizada na fabricação do produto possui uma boa qualidade.

Isso deve ser um hábito no momento da compra de Whey Protein, pois para cada lote do produto, existe um laudo técnico específico.

Ao saber qual é a empresa fornecedora da matéria-prima para o Whey Protein que você está pensando em comprar, é possível pesquisar a procedência da empresa e a qualidade da sua matéria-prima.

A empresa dinamarquesa Arla e a irlandesa Glanbia são as duas maiores referências de empresas fornecedoras de matéria-prima para um suplemento de Whey Protein de excelente qualidade. 

como escolher um bom whey protein

4. EVITE PRODUTOS COM MUITOS ADITIVOS

A composição nutricional é um fator importantíssimo na hora de escolher um Whey Protein de boa qualidade.

Quanto menos aditivos químicos ele possuir na lista de ingredientes, melhor será para os seus resultados e, principalmente, para a sua saúde.

Sendo assim, evite comprar um Whey Protein que contenha ingredientes como maltodextrina, dextrose, açúcar, corantes, saborizantes, aromatizantes, conservantes e adoçantes artificiais.

Essas informações referentes a composição e quantidade dos ingredientes do produto, são descritas no rótulo na ordem de quantidade, começando sempre do ingrediente que possui a maior quantidade, para o que possui a menor.

Isso significa, que quanto antes  esses nomes aparecerem na lista de ingredientes, maior será a quantidade de aditivos químicos  presentes na composição do produto.

Isso não vale apenas para o Whey Protein ou para algum outro suplemento, mas sim, para todos os produtos que são comercializados pela indústria alimentícia.

5. CUSTO X BENEFÍCIO

Na hora de escolher um bom suplemento de Whey Protein, certamente, você também levará em consideração o valor do produto.

Mas a parte boa, é que não necessariamente um suplemento mais caro, possui uma melhor qualidade nutricional. 

Com certeza, se você for em uma loja de suplementos, na grande maioria das vezes, o vendedor vai te oferecer o produto de maior valor, mas isso não será pela melhor qualidade, mas sim, pela maior comissão que ele irá receber.

A verdade, é que o melhor suplemento de Whey Protein é o que foi produzido com uma matéria-prima de qualidade e que possui uma menor quantidade de aditivos químicos na composição.

Além disso, para os mais preocupados com o meio ambiente, hoje em dia já existem as marcas “clean label”, que além de possuírem ingredientes naturais, também fazem questão de extrair a matéria-prima dos seus produtos cuidando do tratamento e da saúde dos animais envolvidos na produção do leite  que e usado para fabricar o Whey Protein.

como escolher um suplemento de whey protein

CONCLUSÃO

Escolher um bom suplemento de Whey Protein, pode até parecer uma tarefa difícil, mas eu tenho certeza, que se você levar em consideração essas dicas, esse processo vai ficar bem mais fácil de ser realizado.

Além disso, o Whey Protein é um suplemento super versátil, que pode ser consumido por pessoas que possuem diferentes objetivos e finalidades.

Então, vale a pena você parar alguns minutos do seu dia pra avaliar com calma as marcas de suplementos existentes no mercado pra fazer a melhor escolha possível, de acordo com às suas reais necessidades.

Lembre-se que – comprar um suplemento se baseando apenas no preço não é uma decisão muito inteligente, pois dependendo do produto escolhido, o “barato” pode acabar custando muito mais caro do que um suplemento que possui uma melhor qualidade.

Espero ter ajudado com essas informações…

Conte comigo sempre que você precisar!

Bruno Motta

REFERÊNCIAS

  1. Carunchia Whetstine ME, Croissant AE, Drake MA. Characterization of dried whey protein concentrate and isolate flavor. J Dairy Sci. (2005)
  2. Off-flavors of whey protein concentrates: A literature review.
  3. Leksrisompong P, et al. Bitter taste inhibiting agents for whey protein hydrolysate and whey protein hydrolysate beverages. J Food Sci. (2012)
  4. Haraguchi T, et al. Synergistic effects of sour taste and low temperature in suppressing the bitterness of Aminoleban® EN. Chem Pharm Bull (Tokyo). (2011)
  5. Levenhagen DK, et al. Postexercise protein intake enhances whole-body and leg protein accretion in humans. Med Sci Sports Exerc. (2002)
  6. Nomenclature of the Proteins of Cows’ Milk—Sixth Revision.
  7. Abd El-Fattah AM, et al. Changes in composition of colostrum of Egyptian buffaloes and Holstein cows. BMC Vet Res. (2012)
  8. Zhang H, et al. Changes in chemical composition of Alxa bactrian camel milk during lactation. J Dairy Sci. (2005)
  9. Morin DE, et al. Composition of milk from llamas in the United States. J Dairy Sci. (1995)
  10. Adkins Y, et al. Changes in nutrient and protein composition of cat milk during lactation. Am J Vet Res. (1997)
  11.  Jenness R. The composition of human milk. Semin Perinatol. (1979)
  12. Ye X, Yoshida S, Ng TB. Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography. Int J Biochem Cell Biol. (2000)
  13. Conti A, et al. Bovine beta-lactoglobulin H: isolation by preparative isoelectric focusing in immobilized pH gradients and preliminary characterization. J Biochem Biophys Methods. (1988)
  14. Godovac-Zimmermann J, et al. Isolation and rapid sequence characterization of two novel bovine beta-lactoglobulins I and J. J Protein Chem. (1996)
  15. Godovac-Zimmermann J, et al. Genetic variants of bovine beta-lactoglobulin. A novel wild-type beta-lactoglobulin W and its primary sequence. Biol Chem Hoppe Seyler. (1990)
  16. Sousa GT, et al. Dietary whey protein lessens several risk factors for metabolic diseases: a review. Lipids Health Dis. (2012)
  17. Heine WE, Klein PD, Reeds PJ. The importance of alpha-lactalbumin in infant nutrition. J Nutr. (1991)
  18. Rapid confirmation and revision of the primary structure of bovineserumalbumin by ESIMS and frit-FAB LC/MS.
  19. Carter DC, Ho JX. Structure of serum albumin. Adv Protein Chem. (1994)
  20. Keogh JB, et al. Effect of glycomacropeptide fractions on cholecystokinin and food intake. Br J Nutr. (2010)
  21. Kissileff HR, et al. C-terminal octapeptide of cholecystokinin decreases food intake in man. Am J Clin Nutr. (1981)
  22. Pi-Sunyer X, et al. C-terminal octapeptide of cholecystokinin decreases food intake in obese men. Physiol Behav. (1982)
  23. Burton-Freeman BM. Glycomacropeptide (GMP) is not critical to whey-induced satiety, but may have a unique role in energy intake regulation through cholecystokinin (CCK). Physiol Behav. (2008)
  24. Legrand D, et al. Lactoferrin structure and functions. Adv Exp Med Biol. (2008)
  25. Duarte DC, et al. The effect of bovine milk lactoferrin on human breast cancer cell lines. J Dairy Sci. (2011)
  26. Riechel P, et al. Analysis of bovine lactoferrin in whey using capillary electrophoresis (CE) and micellar electrokinetic chromatography (MEKC). Adv Exp Med Biol. (1998)
  27. Ballard KD, et al. Acute ingestion of a novel whey-derived peptide improves vascular endothelial responses in healthy individuals: a randomized, placebo controlled trial. Nutr J. (2009)
  28. Ballard KD, et al. Acute effects of ingestion of a novel whey-derived extract on vascular endothelial function in overweight, middle-aged men and women. Br J Nutr. (2012)
  29. Cabanos C, et al. High-level production of lactostatin, a hypocholesterolemic peptide, in transgenic rice using soybean A1aB1b as carrier. Transgenic Res. (2012)
  30. Sindayikengera S, Xia WS. Nutritional evaluation of caseins and whey proteins and their hydrolysates from Protamex. J Zhejiang Univ Sci B. (2006)
  31. Nilsson M, Holst JJ, Björck IM. Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks. Am J Clin Nutr. (2007)
  32. Tienstra PA, et al. Assessment of the capabilities of capillary zone electrophoresis for the determination of hippuric and orotic acid in whey. J Chromatogr. (1992)
  33. Izumi H, et al. Bovine milk contains microRNA and messenger RNA that are stable under degradative conditions. J Dairy Sci. (2012)
  34. Oddy WH, et al. TGF-beta in human milk is associated with wheeze in infancy. J Allergy Clin Immunol. (2003)
  35. Hering NA, et al. Transforming growth factor-ß, a whey protein component, strengthens the intestinal barrier by upregulating claudin-4 in HT-29/B6 cells. J Nutr. (2011)
  36. Bounous G. Whey protein concentrate (WPC) and glutathione modulation in cancer treatment. Anticancer Res. (2000)
  37. Micke P, et al. Oral supplementation with whey proteins increases plasma glutathione levels of HIV-infected patients. Eur J Clin Invest. (2001)
  38. Micke P, Beeh KM, Buhl R. Effects of long-term supplementation with whey proteins on plasma glutathione levels of HIV-infected patients. Eur J Nutr. (2002)
  39. Sekhar RV, et al. Deficient synthesis of glutathione underlies oxidative stress in aging and can be corrected by dietary cysteine and glycine supplementation. Am J Clin Nutr. (2011)
  40. Bounous G, et al. The influence of dietary whey protein on tissue glutathione and the diseases of aging. Clin Invest Med. (1989)
  41. Lands LC, et al. Dietary supplementation with pressurized whey in patients with cystic fibrosis. J Med Food. (2010)
  42. Lands LC, et al. Lymphocyte glutathione levels in children with cystic fibrosis. Chest. (1999)
  43. Grey V, et al. Improved glutathione status in young adult patients with cystic fibrosis supplemented with whey protein. J Cyst Fibros. (2003)
  44. Zavorsky GS, et al. An open-label dose-response study of lymphocyte glutathione levels in healthy men and women receiving pressurized whey protein isolate supplements. Int J Food Sci Nutr. (2007)
  45. Sheikholeslami Vatani D, Ahmadi Kani Golzar F. Changes in antioxidant status and cardiovascular risk factors of overweight young men after six weeks supplementation of whey protein isolate and resistance training. Appetite. (2012)
  46. Wang R. Is H2S a stinky remedy for atherosclerosis. Arterioscler Thromb Vasc Biol. (2009)
  47. Jain SK. L-Cysteine supplementation as an adjuvant therapy for type-2 diabetes. Can J Physiol Pharmacol. (2012)
  48. Jha S, et al. Hydrogen sulfide attenuates hepatic ischemia-reperfusion injury: role of antioxidant and antiapoptotic signaling. Am J Physiol Heart Circ Physiol. (2008)
  49. Beard RS Jr, Bearden SE. Vascular complications of cystathionine ß-synthase deficiency: future directions for homocysteine-to-hydrogen sulfide research. Am J Physiol Heart Circ Physiol. (2011)
  50. Yang G, et al. H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase. Science. (2008)
  51. Jain SK, et al. Low levels of hydrogen sulfide in the blood of diabetes patients and streptozotocin-treated rats causes vascular inflammation. Antioxid Redox Signal. (2010)
  52. Ishigami M, et al. A source of hydrogen sulfide and a mechanism of its release in the brain. Antioxid Redox Signal. (2009)
  53. Shibuya N, et al. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal. (2009)
  54. Vascular Endothelium Expresses 3-Mercaptopyruvate Sulfurtransferase and Produces Hydrogen Sulfide.
  55. Cai WJ, et al. The novel proangiogenic effect of hydrogen sulfide is dependent on Akt phosphorylation. Cardiovasc Res. (2007)
  56. Wang Y, et al. Role of hydrogen sulfide in the development of atherosclerotic lesions in apolipoprotein E knockout mice. Arterioscler Thromb Vasc Biol. (2009)
  57. Whiteman M, et al. Adiposity is a major determinant of plasma levels of the novel vasodilator hydrogen sulphide. Diabetologia. (2010)
  58. Potier M, Tomé D. Comparison of digestibility and quality of intact proteins with their respective hydrolysates. J AOAC Int. (2008)
  59. Alexander DD, Cabana MD. Partially hydrolyzed 100% whey protein infant formula and reduced risk of atopic dermatitis: a meta-analysis. J Pediatr Gastroenterol Nutr. (2010)
  60. Alexander DD, et al. Partially hydrolyzed 100% whey protein infant formula and atopic dermatitis risk reduction: a systematic review of the literature. Nutr Rev. (2010)
  61. von Berg A, et al. Certain hydrolyzed formulas reduce the incidence of atopic dermatitis but not that of asthma: three-year results of the German Infant Nutritional Intervention Study. J Allergy Clin Immunol. (2007)
  62. Pennings B, et al. Whey protein stimulates postprandial muscle protein accretion more effectively than do casein and casein hydrolysate in older men. Am J Clin Nutr. (2011)
  63. Buckley JD, et al. Supplementation with a whey protein hydrolysate enhances recovery of muscle force-generating capacity following eccentric exercise. J Sci Med Sport. (2010)
  64. Characterization of ultrafiltration membranes. Part II — Mass transport measurements for low and high molecular weight synthetic polymers in water solutions.
  65. Marella C, Muthukumarappan K, Metzger LE. Evaluation of commercially available, wide-pore ultrafiltration membranes for production of a-lactalbumin-enriched whey protein concentrate. J Dairy Sci. (2011)
  66. Cheang B, Zydney AL. Separation of alpha-lactalbumin and beta-lactoglobulin using membrane ultrafiltration. Biotechnol Bioeng. (2003)
  67. McDonough FE, et al. Composition and properties of whey protein concentrates from ultrafiltration. J Dairy Sci. (1974)
  68. Hall WL, et al. Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite. Br J Nutr. (2003)
  69. Mishima Y, et al. Gastric emptying of liquid and solid meals at various temperatures: effect of meal temperature for gastric emptying. J Gastroenterol. (2009)
  70. Lorient D, Linden G. Dephosphorylation of bovine casein by milk alkaline phosphatase. J Dairy Res. (1976)
  71. Li-Chan E, Nakai S. Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula. J Dairy Res. (1989)
  72. Mahé S, et al. Gastrojejunal kinetics and the digestion of {15N}beta-lactoglobulin and casein in humans: the influence of the nature and quantity of the protein. Am J Clin Nutr. (1996)
  73. Power O, Hallihan A, Jakeman P. Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Amino Acids. (2009)
  74. Calbet JA, Holst JJ. Gastric emptying, gastric secretion and enterogastrone response after administration of milk proteins or their peptide hydrolysates in humans. Eur J Nutr. (2004)
  75. Boirie Y, et al. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A. (1997)
  76. Tipton KD, et al. Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise. Med Sci Sports Exerc. (2004)
  77. Reitelseder S, 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)
  78. Pal S, Ellis V. The acute effects of four protein meals on insulin, glucose, appetite and energy intake in lean men. Br J Nutr. (2010)
  79. The digestion rate of protein is an independent regulating factor of postprandial protein retention.
  80. Murakami M, et al. Structural analysis of a new anti-hypertensive peptide (beta-lactosin B) isolated from a commercial whey product. J Dairy Sci. (2004)
  81. ^ Tavares T, et al. Novel whey-derived peptides with inhibitory effect against angiotensin-converting enzyme: in vitro effect and stability to gastrointestinal enzymes. Peptides. (2011)
  82.  Tavares T, et al. Acute effect of whey peptides upon blood pressure of hypertensive rats, and relationship with their angiotensin-converting enzyme inhibitory activity. Mol Nutr Food Res. (2012)
  83. Weimann C, Meisel H, Erhardt G. Short communication: bovine kappa-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides. J Dairy Sci. (2009)
  84. Welderufael FT, Gibson T, Jauregi P. Production of angiotensin-I-converting enzyme inhibitory peptides from ß-lactoglobulin- and casein-derived peptides: an integrative approach. Biotechnol Prog. (2012)
  85. Nakamura Y, et al. Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J Dairy Sci. (1995)
  86. Sipola M, et al. Long-term intake of milk peptides attenuates development of hypertension in spontaneously hypertensive rats. J Physiol Pharmacol. (2001)
  87. Murakami I, et al. Enhancement or Suppression of ACE Inhibitory Activity by a Mixture of Tea and Foods for Specified Health Uses (FOSHU) That Are Marketed as “Support for Normal Blood Pressure”. ISRN Pharm. (2011)
  88. Hodgson JM, et al. Long-term effects of a protein-enriched diet on blood pressure in older women. Br J Nutr. (2012)
  89. Lee YM, et al. Effect of a milk drink supplemented with whey peptides on blood pressure in patients with mild hypertension. Eur J Nutr. (2007)
  90. Seppo L, et al. A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects. Am J Clin Nutr. (2003)
  91. Pal S, Ellis V. The chronic effects of whey proteins on blood pressure, vascular function, and inflammatory markers in overweight individuals. Obesity (Silver Spring). (2010)
  92. Pal S, Ellis V. Acute effects of whey protein isolate on blood pressure, vascular function and inflammatory markers in overweight postmenopausal women. Br J Nutr. (2011)
  93. Gentilcore D, et al. Effects of intraduodenal glucose, fat, and protein on blood pressure, heart rate, and splanchnic blood flow in healthy older subjects. Am J Clin Nutr. (2008)
  94. Pal S, Ellis V, Ho S. Acute effects of whey protein isolate on cardiovascular risk factors in overweight, post-menopausal women. Atherosclerosis. (2010)
  95. Holmer-Jensen J, et al. Differential effects of dietary protein sources on postprandial low-grade inflammation after a single high fat meal in obese non-diabetic subjects. Nutr J. (2011)
  96. Koenen RR, et al. Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice. Nat Med. (2009)
  97. Mortensen LS, et al. Differential effects of protein quality on postprandial lipemia in response to a fat-rich meal in type 2 diabetes: comparison of whey, casein, gluten, and cod protein. Am J Clin Nutr. (2009)
  98. Morifuji M, et al. Post-exercise carbohydrate plus whey protein hydrolysates supplementation increases skeletal muscle glycogen level in rats. Amino Acids. (2010)
  99. Kanda A, et al. Dietary Whey Protein Hydrolysates Increase Skeletal Muscle Glycogen Levels via Activation of Glycogen Synthase in Mice. J Agric Food Chem. (2012)
  100. Morifuji M, et al. Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles. J Nutr Sci Vitaminol (Tokyo). (2009)
  101. Fei YJ, et al. cDNA structure, genomic organization, and promoter analysis of the mouse intestinal peptide transporter PEPT1. Biochim Biophys Acta. (2000)
  102. Chitapanarux T, et al. Open-labeled pilot study of cysteine-rich whey protein isolate supplementation for nonalcoholic steatohepatitis patients. J Gastroenterol Hepatol. (2009)
  103. Rains JL, Jain SK. Oxidative stress, insulin signaling, and diabetes. Free Radic Biol Med. (2011)
  104. Dröge W. Oxidative stress and ageing: is ageing a cysteine deficiency syndrome. Philos Trans R Soc Lond B Biol Sci. (2005)
  105. Haber CA, et al. N-acetylcysteine and taurine prevent hyperglycemia-induced insulin resistance in vivo: possible role of oxidative stress. Am J Physiol Endocrinol Metab. (2003)
  106. Blouet C, et al. Meal cysteine improves postprandial glucose control in rats fed a high-sucrose meal. J Nutr Biochem. (2007)
  107. Blouet C, et al. Dietary cysteine alleviates sucrose-induced oxidative stress and insulin resistance. Free Radic Biol Med. (2007)
  108. ^ Song D, Hutchings S, Pang CC. Chronic N-acetylcysteine prevents fructose-induced insulin resistance and hypertension in rats. Eur J Pharmacol. (2005)
  109. Diniz YS, et al. Effects of N-acetylcysteine on sucrose-rich diet-induced hyperglycaemia, dyslipidemia and oxidative stress in rats. Eur J Pharmacol. (2006)
  110. Jain SK, et al. L-cysteine supplementation lowers blood glucose, glycated hemoglobin, CRP, MCP-1, and oxidative stress and inhibits NF-kappaB activation in the livers of Zucker diabetic rats. Free Radic Biol Med. (2009)
  111. Supplementation of N-acetylcysteine inhibits NF?B activation and protects against alloxan-induced diabetes in CD-1 mice.
  112. Pieper GM, Siebeneich W. Oral administration of the antioxidant, N-acetylcysteine, abrogates diabetes-induced endothelial dysfunction. J Cardiovasc Pharmacol. (1998)
  113. Prevention of glucose toxicity in HIT-T15 cells and Zucker diabetic fatty rats by antioxidants.
  114. Kaneto H, et al. Beneficial effects of antioxidants in diabetes: possible protection of pancreatic beta-cells against glucose toxicity. Diabetes. (1999)
  115. Frid AH, et al. Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects. Am J Clin Nutr. (2005)
  116. Abrahão V. Nourishing the dysfunctional gut and whey protein. Curr Opin Clin Nutr Metab Care. (2012)
  117. Liu X, et al. Whey protein potentiates the intestinotrophic action of glucagon-like peptide-2 in parenterally fed rats. Am J Physiol Regul Integr Comp Physiol. (2009)
  118. Ten Have GA, et al. Absence of post-prandial gut anabolism after intake of a low quality protein meal. Clin Nutr. (2012)
  119. Benjamin J, et al. Glutamine and whey protein improve intestinal permeability and morphology in patients with Crohn’s disease: a randomized controlled trial. Dig Dis Sci. (2012)
  120. Bortolotti M, et al. Effects of a whey protein supplementation on intrahepatocellular lipids in obese female patients. Clin Nutr. (2011)
  121. Elattar G, et al. The use of whey protein concentrate in management of chronic hepatitis C virus – a pilot study. Arch Med Sci. (2010)
  122. Hamad EM, et al. Protective effect of whey proteins against nonalcoholic fatty liver in rats. Lipids Health Dis. (2011)
  123. Haraguchi FK, et al. Whey protein precludes lipid and protein oxidation and improves body weight gain in resistance-exercised rats. Eur J Nutr. (2011)
  124. Poortmans JR, Dellalieux O. Do regular high protein diets have potential health risks on kidney function in athletes. Int J Sport Nutr Exerc Metab. (2000)
  125. Friedman AN, et al. Comparative effects of low-carbohydrate high-protein versus low-fat diets on the kidney. Clin J Am Soc Nephrol. (2012)
  126. Brinkworth GD, et al. Renal function following long-term weight loss in individuals with abdominal obesity on a very-low-carbohydrate diet vs high-carbohydrate diet. J Am Diet Assoc. (2010)
  127. Cornish SM, et al. Conjugated linoleic acid combined with creatine monohydrate and whey protein supplementation during strength training. Int J Sport Nutr Exerc Metab. (2009)
  128. Kasiske BL, et al. Effects of carbohydrate restriction on renal injury in the obese Zucker rat. Am J Clin Nutr. (1986)
  129. Effect on renal haemodynamics, glomerular filtration rate and albumin excretion of high oral protein load.
  130. Kontessis P, et al. Renal, metabolic and hormonal responses to ingestion of animal and vegetable proteins. Kidney Int. (1990)
  131. Kontessis PA, et al. Renal, metabolic, and hormonal responses to proteins of different origin in normotensive, nonproteinuric type I diabetic patients. Diabetes Care. (1995)
  132. Wiseman MJ, et al. Dietary composition and renal function in healthy subjects. Nephron. (1987)
  133. PULLMAN TN, et al. The influence of dietary protein intake on specific renal functions in normal man. J Lab Clin Med. (1954)
  134. Brändle E, Sieberth HG, Hautmann RE. Effect of chronic dietary protein intake on the renal function in healthy subjects. Eur J Clin Nutr. (1996)
  135. Effect of protein-restricted diet on renal response to a meat meal in humans.
  136. Skov AR, et al. Changes in renal function during weight loss induced by high vs low-protein low-fat diets in overweight subjects. Int J Obes Relat Metab Disord. (1999)
  137. Friedman AN. High-protein diets: potential effects on the kidney in renal health and disease. Am J Kidney Dis. (2004)
  138. Brenner BM, Meyer TW, Hostetter TH. Dietary protein intake and the progressive nature of kidney disease: the role of hemodynamically mediated glomerular injury in the pathogenesis of progressive glomerular sclerosis in aging, renal ablation, and intrinsic renal disease. N Engl J Med. (1982)
  139. Ambühl PM. Protein intake in renal and hepatic disease. Int J Vitam Nutr Res. (2011)
  140. Markus CR, et al. The bovine protein alpha-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. Am J Clin Nutr. (2000)
  141. Citraro R, et al. Preclinical activity profile of a-lactoalbumin, a whey protein rich in tryptophan, in rodent models of seizures and epilepsy. Epilepsy Res. (2011)
  142. Mainardi P, Leonardi A, Albano C. Potentiation of brain serotonin activity may inhibit seizures, especially in drug-resistant epilepsy. Med Hypotheses. (2008)
  143. Errichiello L, et al. A proof-of-concept trial of the whey protein alfa-lactalbumin in chronic cortical myoclonus. Mov Disord. (2011)
  144. Rusu D, et al. A bovine whey protein extract can enhance innate immunity by priming normal human blood neutrophils. J Nutr. (2009)
  145. Migliore-Samour D, et al. Effects of tripeptides derived from milk proteins on polymorphonuclear oxidative and phosphoinositide metabolisms. Biochem Pharmacol. (1992)
  146. Li EW, Mine Y. Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human macrophagelike cells, U937. J Agric Food Chem. (2004)
  147. Wong KF, et al. Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions. J Dairy Sci. (1998)
  148. Ebert EC, Roberts AI. Lamina propria lymphocytes produce interferon-gamma and develop suppressor activity in response to lactoglobulin. Dig Dis Sci. (2001)
  149. Wong CW, et al. Effects of purified bovine whey factors on cellular immune functions in ruminants. Vet Immunol Immunopathol. (1997)
  150. Bovine Glycomacropeptide Is Anti-Inflammatory in Rats with Hapten-Induced Colitis.
  151.  Zemel MB, et al. Effects of dairy compared with soy on oxidative and inflammatory stress in overweight and obese subjects. Am J Clin Nutr. (2010)
  152. Panagiotakos DB, et al. Dairy products consumption is associated with decreased levels of inflammatory markers related to cardiovascular disease in apparently healthy adults: the ATTICA study. J Am Coll Nutr. (2010)
  153. Kennedy RS, et al. The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: a phase I-II clinical study. Anticancer Res. (1995)
  154. Kanwar JR, et al. ‘Iron-saturated’ lactoferrin is a potent natural adjuvant for augmenting cancer chemotherapy. Immunol Cell Biol. (2008)
  155. Burrow H, Kanwar RK, Kanwar JR. Antioxidant enzyme activities of iron-saturated bovine lactoferrin (Fe-bLf) in human gut epithelial cells under oxidative stress. Med Chem. (2011)
  156. Roseanu A, et al. Liposomalization of lactoferrin enhanced its anti-tumoral effects on melanoma cells. Biometals. (2010)
  157. Castro GA, et al. In vitro impact of a whey protein isolate (WPI) and collagen hydrolysates (CHs) on B16F10 melanoma cells proliferation. J Dermatol Sci. (2009)
  158. Xu XX, et al. Apoptosis of stomach cancer cell SGC-7901 and regulation of Akt signaling way induced by bovine lactoferrin. J Dairy Sci. (2010)
  159. Li D, et al. Binding of lactoferrin to IGBP1 triggers apoptosis in a lung adenocarcinoma cell line. Anticancer Res. (2011)
  160. Furlong SJ, Mader JS, Hoskin DW. Bovine lactoferricin induces caspase-independent apoptosis in human B-lymphoma cells and extends the survival of immune-deficient mice bearing B-lymphoma xenografts. Exp Mol Pathol. (2010)
  161. Kozu T, et al. Effect of orally administered bovine lactoferrin on the growth of adenomatous colorectal polyps in a randomized, placebo-controlled clinical trial. Cancer Prev Res (Phila). (2009)
  162. Tsuda H, et al. Cancer prevention by bovine lactoferrin: from animal studies to human trial. Biometals. (2010)
  163. Gibbons JA, Kanwar RK, Kanwar JR. Lactoferrin and cancer in different cancer models. Front Biosci (Schol Ed). (2011)
  164. Dillon EL, et al. Cancer cachexia and anabolic interventions: a case report. J Cachexia Sarcopenia Muscle. (2012)
  165. ^ Deutz NE, et al. Muscle protein synthesis in cancer patients can be stimulated with a specially formulated medical food. Clin Nutr. (2011)
  166. Hulmi JJ, et al. 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. Eur J Appl Physiol. (2008)
  167. Hulmi JJ, et al. Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men. J Appl Physiol. (2009)
  168. Hulmi JJ, et al. Acute and long-term effects of resistance exercise with or without protein ingestion on muscle hypertrophy and gene expression. Amino Acids. (2009)
  169. Bunn JA, et al. Protein and Amino Acid Supplementation Does Not Alter Proteolytic Gene Expression following Immobilization. J Nutr Metab. (2011)
  170. Moore DR, et al. Resistance exercise enhances mTOR and MAPK signalling in human muscle over that seen at rest after bolus protein ingestion. Acta Physiol (Oxf). (2011)
  171. ^ Biolo G, et al. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am J Physiol. (1997)
  172. Postexercise net protein synthesis in human muscle from orally administered amino acids.
  173. Burd NA, et al. Enhanced amino acid sensitivity of myofibrillar protein synthesis persists for up to 24 h after resistance exercise in young men. J Nutr. (2011)
  174. Yang Y, et al. Resistance exercise enhances myofibrillar protein synthesis with graded intakes of whey protein in older men. Br J Nutr. (2012)
  175. Moore DR, et al. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. (2009)
  176. Hoffman JR, et al. Effect of protein-supplement timing on strength, power, and body-composition changes in resistance-trained men. Int J Sport Nutr Exerc Metab. (2009)
  177. Kerksick CM, et al. The effects of protein and amino acid supplementation on performance and training adaptations during ten weeks of resistance training. J Strength Cond Res. (2006)
  178. Andersen LL, et al. The effect of resistance training combined with timed ingestion of protein on muscle fiber size and muscle strength. Metabolism. (2005)
  179. Hartman JW, 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. Am J Clin Nutr. (2007)
  180.  Weisgarber KD, Candow DG, Vogt E SM. Whey Protein Before and During Resistance Exercise Has No Effect on Muscle Mass and Strength in Untrained Young Adults. Int J Sport Nutr Exerc Metab. (2012)
  181. Kukuljan S, et al. Effects of resistance exercise and fortified milk on skeletal muscle mass, muscle size, and functional performance in middle-aged and older men: an 18-mo randomized controlled trial. J Appl Physiol. (2009)
  182. Candow DG, et al. Protein supplementation before and after resistance training in older men. Eur J Appl Physiol. (2006)
  183. Weinheimer EM, et al. Whey protein supplementation does not affect exercise training-induced changes in body composition and indices of metabolic syndrome in middle-aged overweight and obese adults. J Nutr. (2012)
  184. Dangin M, et al. The rate of protein digestion affects protein gain differently during aging in humans. J Physiol. (2003)
  185. ^ a b c Dideriksen KJ, et al. Stimulation of muscle protein synthesis by whey and caseinate ingestion after resistance exercise in elderly individuals. Scand J Med Sci Sports. (2011)
  186. Wycherley TP, et al. Timing of protein ingestion relative to resistance exercise training does not influence body composition, energy expenditure, glycaemic control or cardiometabolic risk factors in a hypocaloric, high protein diet in patients with type 2 diabetes. Diabetes Obes Metab. (2010)
  187. Esmarck B, et al. Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans. J Physiol. (2001)
  188. Jordan LY, et al. Nitrogen balance in older individuals in energy balance depends on timing of protein intake. J Gerontol A Biol Sci Med Sci. (2010)
  189. Tipton KD, et al. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am J Physiol Endocrinol Metab. (2001)
  190. An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise.
  191. Levenhagen DK, et al. Postexercise nutrient intake timing in humans is critical to recovery of leg glucose and protein homeostasis. Am J Physiol Endocrinol Metab. (2001)
  192. Hoffman JR, et al. Effect of a proprietary protein supplement on recovery indices following resistance exercise in strength/power athletes. Amino Acids. (2010)
  193. Etheridge T, Philp A, Watt PW. A single protein meal increases recovery of muscle function following an acute eccentric exercise bout. Appl Physiol Nutr Metab. (2008)
  194. Ratamess NA, et al. The effects of amino acid supplementation on muscular performance during resistance training overreaching. J Strength Cond Res. (2003)
  195. Nosaka K, Sacco P, Mawatari K. Effects of amino acid supplementation on muscle soreness and damage. Int J Sport Nutr Exerc Metab. (2006)
  196. Shimomura Y, et al. Nutraceutical effects of branched-chain amino acids on skeletal muscle. J Nutr. (2006)
  197. Bouthegourd JC, et al. A preexercise alpha-lactalbumin-enriched whey protein meal preserves lipid oxidation and decreases adiposity in rats. Am J Physiol Endocrinol Metab. (2002)
  198. Lorenzen J, et al. The effect of milk proteins on appetite regulation and diet-induced thermogenesis. Eur J Clin Nutr. (2012)
  199. Hackney KJ, Bruenger AJ, Lemmer JT. Timing protein intake increases energy expenditure 24 h after resistance training. Med Sci Sports Exerc. (2010)
  200. Baer DJ, et al. Whey protein but not soy protein supplementation alters body weight and composition in free-living overweight and obese adults. J Nutr. (2011)
  201. Khalil DA, et al. Soy protein supplementation increases serum insulin-like growth factor-I in young and old men but does not affect markers of bone metabolism. J Nutr. (2002)
  202. Zhou J, et al. Dietary whey protein decreases food intake and body fat in rats. Obesity (Silver Spring). (2011)
  203. Lam SM, et al. The influence of whey protein and glycomacropeptide on satiety in adult humans. Physiol Behav. (2009)
  204. Luhovyy BL, Akhavan T, Anderson GH. Whey proteins in the regulation of food intake and satiety. J Am Coll Nutr. (2007)
  205. Abou Samra R, et al. Effect of different protein sources on satiation and short-term satiety when consumed as a starter. Nutr J. (2011)
  206. ^ a b Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults.
  207. Poppitt SD, et al. Low-dose whey protein-enriched water beverages alter satiety in a study of overweight women. Appetite. (2011)
  208. Astbury NM, et al. Dose-response effect of a whey protein preload on within-day energy intake in lean subjects. Br J Nutr. (2010)
  209. Frestedt JL, et al. A whey-protein supplement increases fat loss and spares lean muscle in obese subjects: a randomized human clinical study. Nutr Metab (Lond). (2008)
  210. Zhu K, et al. The effects of a two-year randomized, controlled trial of whey protein supplementation on bone structure, IGF-1, and urinary calcium excretion in older postmenopausal women. J Bone Miner Res. (2011)
  211. ^ Rennie MJ, et al. Control of the size of the human muscle mass. Annu Rev Physiol. (2004)
  212. Cuthbertson D, et al. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J. (2005)
  213. Nutrient signalling in the regulation of human muscle protein synthesis.
  214. Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia.
  215. Tang JE, et al. 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. (2009)
  216. Whey protein stimulates postprandial muscle protein accretion more effectively than do casein and casein hydrolysate in older men.
  217. Dangin M, et al. The digestion rate of protein is an independent regulating factor of postprandial protein retention. Am J Physiol Endocrinol Metab. (2001)
  218. Engelen MP, et al. Casein protein results in higher prandial and exercise induced whole body protein anabolism than whey protein in Chronic Obstructive Pulmonary Disease. Metabolism. (2012)
  219. Pal S, Ellis V, Dhaliwal S. Effects of whey protein isolate on body composition, lipids, insulin and glucose in overweight and obese individuals. Br J Nutr. (2010)
  220. Haraguchi FK, et al. Evaluation of biological and biochemical quality of whey protein. J Med Food. (2010)
  221. de Aguilar-Nascimento JE, Prado Silveira BR, Dock-Nascimento DB. Early enteral nutrition with whey protein or casein in elderly patients with acute ischemic stroke: a double-blind randomized trial. Nutrition. (2011)
  222. Candow DG, et al. Effect of whey and soy protein supplementation combined with resistance training in young adults. Int J Sport Nutr Exerc Metab. (2006)
  223. Hays NP, et al. Effects of whey and fortified collagen hydrolysate protein supplements on nitrogen balance and body composition in older women. J Am Diet Assoc. (2009)
  224. Howarth KR, et al. Coingestion of protein with carbohydrate during recovery from endurance exercise stimulates skeletal muscle protein synthesis in humans. J Appl Physiol. (2009)
  225. Breen L, et al. The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis. J Physiol. (2011)
  226. Koopman R, et al. Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects. Am J Physiol Endocrinol Metab. (2005)
  227. Koopman R, et al. Co-ingestion of leucine with protein does not further augment post-exercise muscle protein synthesis rates in elderly men. Br J Nutr. (2008)
  228. Koopman R, et al. Co-ingestion of protein and leucine stimulates muscle protein synthesis rates to the same extent in young and elderly lean men. Am J Clin Nutr. (2006)
  229. Churchward-Venne TA, 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. J Physiol. (2012)
  230. Rodondi A, et al. Zinc increases the effects of essential amino acids-whey protein supplements in frail elderly. J Nutr Health Aging. (2009)
  231. Chevalley T, et al. Early serum IGF-I response to oral protein supplements in elderly women with a recent hip fracture. Clin Nutr. (2010)
  232. Schürch MA, et al. Protein supplements increase serum insulin-like growth factor-I levels and attenuate proximal femur bone loss in patients with recent hip fracture. A randomized, double-blind, placebo-controlled trial. Ann Intern Med. (1998)
  233. Oben J, Kothari SC, Anderson ML. An open label study to determine the effects of an oral proteolytic enzyme system on whey protein concentrate metabolism in healthy males. J Int Soc Sports Nutr. (2008)
  234. Pettersson-Kastberg J, et al. alpha-Lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: a new biological function resulting from partial unfolding. J Mol Biol. (2009)
  235. Apoptosis induced by a human milk protein.
  236. Svensson M, et al. Conversion of alpha-lactalbumin to a protein inducing apoptosis. Proc Natl Acad Sci U S A. (2000)
  237. Permyakov SE, et al. A novel method for preparation of HAMLET-like protein complexes. Biochimie. (2011)
  238. Hakansson AP, et al. Apoptosis-like death in bacteria induced by HAMLET, a human milk lipid-protein complex. PLoS One. (2011)
  239. Svensson M, et al. Hamlet–a complex from human milk that induces apoptosis in tumor cells but spares healthy cells. Adv Exp Med Biol. (2002)
  240. Permyakov SE, et al. Oleic acid is a key cytotoxic component of HAMLET-like complexes. Biol Chem. (2012)
  241. Lisková K, et al. Effect of denaturation of alpha-lactalbumin on the formation of BAMLET (bovine alpha-lactalbumin made lethal to tumor cells). J Agric Food Chem. (2010)
  242. Pettersson J, Mossberg AK, Svanborg C. alpha-Lactalbumin species variation, HAMLET formation, and tumor cell death. Biochem Biophys Res Commun. (2006)
  243. Brinkmann CR, et al. Preparation and comparison of cytotoxic complexes formed between oleic acid and either bovine or human a-lactalbumin. J Dairy Sci. (2011)
  244. Optimization of thermal pretreatment conditions for the separation of native alpha-lactalbumin from whey protein concentrates by means of selective denaturation of beta-lactoglobulin.
  245. Fast J, et al. Stability of HAMLET–a kinetically trapped alpha-lactalbumin oleic acid complex. Protein Sci. (2005)
  246. Khan S, et al. Investigation of Short-term Variations in Casein and Whey Proteins in Breast Milk of Term Mothers. J Pediatr Gastroenterol Nutr. (2012)
  247. Liao Y, et al. Proteomic characterization of human milk whey proteins during a twelve-month lactation period. J Proteome Res. (2011)
  248. Osborn DA, Sinn J. Formulas containing hydrolysed protein for prevention of allergy and food intolerance in infants. Cochrane Database Syst Rev. (2006)
  249. Kucia M, et al. High-protein diet during gestation and lactation affects mammary gland mRNA abundance, milk composition and pre-weaning litter growth in mice. Animal. (2011)
  250. Mojtahedi MC, et al. The effects of a higher protein intake during energy restriction on changes in body composition and physical function in older women. J Gerontol A Biol Sci Med Sci. (2011)
  251. Pennings B, et al. Amino acid absorption and subsequent muscle protein accretion following graded intakes of whey protein in elderly men. Am J Physiol Endocrinol Metab. (2012)
  252. Wolfe RR. The underappreciated role of muscle in health and disease. Am J Clin Nutr. (2006)
  253. Cordero-MacIntyre ZR, et al. Reproducibility of DXA in obese women. J Clin Densitom. (2002)
  254. Phillips SM. The science of muscle hypertrophy: making dietary protein count. Proc Nutr Soc. (2011)
  255. Dangin M, et al. Influence of the protein digestion rate on protein turnover in young and elderly subjects. J Nutr. (2002)
  256. Mitchell CJ, et al. Acute post-exercise myofibrillar protein synthesis is not correlated with resistance training-induced muscle hypertrophy in young men. PLoS One. (2014)
  257. Greenhaff PL, et al. Disassociation between the effects of amino acids and insulin on signaling, ubiquitin ligases, and protein turnover in human muscle. Am J Physiol Endocrinol Metab. (2008)
  258. Jespersen JG, et al. Activated protein synthesis and suppressed protein breakdown signaling in skeletal muscle of critically ill patients. PLoS One. (2011)
  259. Lacey JM, Wilmore DW. Is glutamine a conditionally essential amino acid?. Nutr Rev. (1990)
  260. Antonio J, Street C. Glutamine: a potentially useful supplement for athletes. Can J Appl Physiol. (1999)
  261. Antonio J, et al. The effects of high-dose glutamine ingestion on weightlifting performance. J Strength Cond Res. (2002)
  262. Candow DG, et al. Effect of glutamine supplementation combined with resistance training in young adults. Eur J Appl Physiol. (2001)
  263. Finn KJ, Lund R, Rosene-Treadwell M. Glutamine Supplementation did not Benefit Athletes During Short-Term Weight Reduction. J Sports Sci Med. (2003)
  264. Ramezani Ahmadi A, et al. The effect of glutamine supplementation on athletic performance, body composition, and immune function: A systematic review and a meta-analysis of clinical trials. Clin Nutr. (2018)
  265. Bernfeld E, et al. Phospholipase D-Dependent mTORC1 Activation by Glutamine. Journal of Biological Chemistry. (2018)
  266. Street B, Byrne C, Eston R. Glutamine Supplementation in Recovery From Eccentric Exercise Attenuates Strength Loss and Muscle Soreness. Journal of Exercise Science and Fitness. (2011)
  267. Rahmani Nia F, et al. Effect of L-glutamine supplementation on electromyographic activity of the quadriceps muscle injured by eccentric exercise. Iran J Basic Med Sci. (2013)
  268. Waldron M, et al. The effects of acute leucine or leucine-glutamine co-ingestion on recovery from eccentrically biased exercise. Amino Acids. (2018)
  269. Legault Z, Bagnall N, Kimmerly DS. The Influence of Oral L-Glutamine Supplementation on Muscle Strength Recovery and Soreness Following Unilateral Knee Extension Eccentric Exercise. Int J Sport Nutr Exerc Metab. (2015)
  270. Li P, et al. Amino acids and immune function. Br J Nutr. (2007)
  271. Castell LM. Can glutamine modify the apparent immunodepression observed after prolonged, exhaustive exercise?. Nutrition. (2002)
  272. Castell LM, Poortmans JR, Newsholme EA. Does glutamine have a role in reducing infections in athletes?. Eur J Appl Physiol Occup Physiol. (1996)
  273. Krzywkowski K, et al. Effect of glutamine supplementation on exercise-induced changes in lymphocyte function. Am J Physiol Cell Physiol. (2001)
  274. Walsh NP, et al. Effect of oral glutamine supplementation on human neutrophil lipopolysaccharide-stimulated degranulation following prolonged exercise. Int J Sport Nutr Exerc Metab. (2000)
  275. Krzywkowski K, et al. Effect of glutamine and protein supplementation on exercise-induced decreases in salivary IgA. J Appl Physiol (1985). (2001)
  276. Hiscock N, Pedersen BK. Exercise-induced immunodepression- plasma glutamine is not the link. J Appl Physiol (1985). (2002)
  277. Dokladny K, Zuhl MN, Moseley PL. Intestinal epithelial barrier function and tight junction proteins with heat and exercise. J Appl Physiol (1985). (2016)
  278. Pugh JN, et al. Glutamine supplementation reduces markers of intestinal permeability during running in the heat in a dose-dependent manner. Eur J Appl Physiol. (2017)
  279. Zuhl M, et al. The effects of acute oral glutamine supplementation on exercise-induced gastrointestinal permeability and heat shock protein expression in peripheral blood mononuclear cells. Cell Stress Chaperones. (2015)
  280. Macfarlane GT, Macfarlane S. Bacteria, colonic fermentation, and gastrointestinal health. J AOAC Int. (2012)
  281. MacLean DA, Graham TE, Saltin B. Branched-chain amino acids augment ammonia metabolism while attenuating protein breakdown during exercise. Am J Physiol. (1994)
  282. Joint WHO/FAO/UNU Expert Consultation. Protein and Amino Acid Requirements in Human Nutrition. World Health Organ Tech Rep Ser. (2007)
  283. Douglas S Kalman. Amino Acid Composition of an Organic Brown Rice Protein Concentrate and Isolate Compared to Soy and Whey Concentrates and Isolates. Foods. (2014)
  284. Stefan H M Gorissen, et al. Protein Content and Amino Acid Composition of Commercially Available Plant-Based Protein Isolates. Amino Acids. (2018)
  285. EASTOE JE. The amino acid composition of mammalian collagen and gelatin. Biochem J. (1955)
  286. Zdzieblik D, et al. Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: a randomised controlled trial. Br J Nutr. (2015)
  287. Mathai JK, Liu Y, Stein HH. Values for digestible indispensable amino acid scores (DIAAS) for some dairy and plant proteins may better describe protein quality than values calculated using the concept for protein digestibility-corrected amino acid scores (PDCAAS). Br J Nutr. (2017)

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