Ultra Whey Protein Isolate

Front bag image of Ultra Whey Protein Isolate from Z Natural Foods 5 lb

Back of the bag image of Ultra Whey Protein Isolate from Z Natural Foods 5 lb

Front and back label image of Ultra Whey Protein Isolate from Z Natural Foods Bulk size

Image of Ultra Whey Protein Isolate powder in plastic measuring cup on white background

Ultra Whey Protein Isolate

Pay Now

£17.73

As low as

Weight

1 lb

5 lbs

44 lbs

1 lbs

5 lb

Flavor

Chocolate Caramel Cappuccino

Organic Chocolate Whey Concentrate

Chocolate Whey Isolate

Goat Whey

Mocha Whey Isolate

Vanilla Whey Concentrate

Organic Whey Concentrate

Whey Isolate

Vanilla Whey Isolate

Whey Concentrate

Organic Whey Isolate

About Product

Whey protein isolate is a concentrated form of whey protein, the liquid part of milk that separates during cheese production.

First discovered in the early 1900s, whey protein isolate is a source of essential amino acids, which are the building blocks of proteins.

It is low in lactose, fat, and cholesterol, making it a popular choice for those looking to support lean muscle mass and their overall health.

Whey protein isolate is commonly used in protein shakes, smoothies, and other protein-rich foods. It can also be added to meals and snacks for some extra protein.

In addition to its protein content, whey protein isolate contains various vitamins and minerals, including calcium, magnesium, and phosphorus.

Please Note: Due to recent market conditions, whey protein prices have surged significantly beyond our control. We remain dedicated to maintaining the highest quality and will adjust prices down as soon as market values stabilize. Thank you for your understanding and continued support.

Protein Profile (Percent of Total Protein):

Beta-Lactoglobulin - 50%
Alpha-Lactalbumin - 22%
Bovine Serum Albumin - 2.0%
Immunoglobulin - 4.0%
Lactoferrin - <1.0%
Lactoperoxidase - <1.0%
Glycomacropeptide - 20%

Allergens: Milk

Our Ultra Whey Isolate is instantized, with a small amount of non-GMO sunflower lecithin, which means it will mix in liquid much easier than whey concentrates, which are not instantized.

Suggested Use:

Mix 6 level tablespoons / 1 ounce (28 grams ) with 12 ounces of cold water, skim milk, or juice and thoroughly mix in a blender, shaker, or fork for 20-30 seconds. For best results, consume 1-2 servings daily, with one serving post-exercise. It can also be blended into your favorite smoothie.

Mixing suggestions: To increase flavor and nutritional profile, combine with our organic extra-rich cacao, banana flakes, and strawberry powder.

Miscellaneous Facts about our Whey Protein Isolate Powder

Ingredients: Whey Protein Isolate, <1% Lecithin (derived from non-GMO sunflower).

Other Names: Bovine Whey Protein Isolate, Concentre de Proteine de Petit-Lait Bovin, Fraction de Lactoserum, Fraction de Petit-Lait, Isolat de Proteine de Lactoserum, Isolat de Proteine de Petit-Lait, Lactoserum de Lait de ChÃ¨vre, MBP, Milk Protein, Milk Protein Isolate, Mineral Whey Isolate, ProteÃnas del Suero de la Leche, Proteine de Lactoserum, Proteine de Lait, Proteine de Petit-Lait, Whey, Whey Fraction, Whey Peptides, Whey Isolate, WPI.

Origin: Raised and processed in the USA. Packaged with care in Florida, USA.

How to Maintain Optimum Freshness

This product is packaged in airtight stand-up, resealable foil pouches for optimum freshness.
Once opened, push the air out of the pouch before resealing it to preserve maximum potency.
Keep your powder in a cool, dark, dry place.

This product is 100% natural and minimally processed:

Taste, smell, texture, and color vary from batch to batch. Go here to learn why our products may naturally vary.

The important protections we take to bring you safe and nutritious superfoods:

Please go here to discover the essential steps we take to deliver fresh, quality nutrition.

Bulk Quantities?

Need to order a large quantity of our products? We are happy to help! Please get in touch with our Bulk department to discuss the details.

* Product packaging, pictures, and origin may vary.

Sources & References

1. Valerio A, D"'Antona G, Nisoli E. Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evolutionary perspective. Aging (Albany NY). 2011 May;3(5):464-78.

2. D"'Antona G, Ragni M, Cardile A, et al. Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab. 2010 October;12(4):362-72.

3. Alvers AL, Fishwick LK, Wood MS, Hu D, Chung HS, Dunn WA, and Aris JP. Autophagy and amino acid homeostasis are required for chronological longevity in Saccharomyces cerevisiae. Aging Cell. 2009;8:353-69.

4. Fuchs S, Bundy JG, Davies SK, Viney JM, Swire JS, and Leroi AM. A metabolic signature of long life in Caenorhabditis elegans. BMC Biol. 2010;8:14.

5. YalÃ§in AS. Emerging therapeutic potential of whey proteins and peptides. Curr Pharm Des. 2006;12(13):1637-43.

6. Krissansen GW. Emerging health properties of whey proteins and their clinical implications. J Am Coll Nutr. Dec. 2007;26(6):713S-23S.

7. Vegarud GE, Langsrud T, Svenning C. Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br J Nutr. 2000;84(Suppl 1):S91-8.

8. Available at: http://www.innovatewithdairy.com/SiteCollectionDocuments/Mono_Immunity_0304.pdf. Accessed June 12, 2013.

9. Kent KD, Harper WJ, Bomser JA. Effect of whey protein isolates on intracellular glutathione and oxidant-induced cell death in human prostate epithelial cells. Toxicol In Vitro. 2003 Feb;17(1):27-33.

10. Bounous G, Gervais F, Amer V, Batist G, Gold P. The influence of dietary whey protein on tissue glutathione and the diseases of aging. Clin Invest Med. 1989;12:343-9.

11. Townsend DM, Tew KD, Tapiero H. The importance of glutathione in human disease. Biomed Pharmacother. 2003 May-Jun;57(3-4):145-55.

12. Wu G, Fang YZ, Yang S, Lupton JR, Turner ND. Glutathione metabolism and its implications for health. J Nutr. 2004 Mar;134(3):489-92.

13. Katsanos CS, Chinkes DL, Paddon-Jones D, Zhang XJ, Aarsland A, Wolfe RR. Whey protein ingestion in elderly persons results in greater muscle protein accrual than ingestion of its constituent essential amino acid content. Nutr Res. 2008 Oct;28(10):651-8.

14. Bounous G, Batist G, Gold P. Immunoenhancing property of dietary whey protein in mice: role of glutathione. Clin Invest Med. 1989 Jun;12(3):154-61.

15. Currais A, Maher P. Functional consequences of age-dependent changes in glutathione status in the brain. Antioxid Redox Signal. 2013 Feb 5. [Epub ahead of print]

16. Shertzer HG, Woods SE, Krishan M, Genter MB, Pearson KJ. Dietary whey protein lowers the risk for metabolic disease in mice fed a high-fat diet. J Nutr. 2011 Apr 1;141(4):582-7.

17. Paddon-Jones D, Short KR, Campbell WW, Volpi E, Wolfe RR. Role of dietary protein in the sarcopenia of aging. Am J Clin Nutr. 2008 May;87(5):1562S-6S.

18. Pepe G, Tenore GC, Mastrocinque R, Stusio P, Campiglia P. Potential anticarcinogenic peptides from bovine milk. J Amino Acids. 2013;2013:939804.

19. 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 Jun;75(6):1051-6.

20. Visvanathan R, and Chapman IM. Undernutrition and anorexia in the older person. Gastroenterol Clin North Am. 2009;38:393-409.

21. Ahmed T, and Haboubi N. Assessment and management of nutrition in older people and its importance to health. Clin Interv Aging. 2010;5:207-16.

22. Chapman IM. Nutritional disorders in the elderly. Med Clin North Am. 2006;90:887-907.

23. Ahmed N, Mandel R, and Fain MJ. Frailty: An emerging geriatric syndrome. Am J Med. 2007;120:748-53.

24. Heilbronn LK, de Jonge L, Frisard MI, et al. Effect of 6-month calorie restriction on biomarkers of longevity, metabolic adaptation, and oxidative stress in overweight individuals: A randomized controlled trial. JAMA. 2006;295:1539-48.

25. Ingram DK, Roth GS. Glycolytic inhibition as a strategy for developing calorie restriction mimetics. Exp Gerontol. 2011;46:148-54.

26. Ingram DK, Zhu M, Mamczarz J, et al. Calorie restriction mimetics: an emerging research field. Aging Cell. 2006 Apr;5(2):97-108.

27. Solerte SB, Gazzaruso C, Bonacasa R, et al. Nutritional supplements with oral amino acid mixtures increases whole-body lean mass and insulin sensitivity in elderly subjects with sarcopenia. Am J Cardiol. 2008;101:69E-77E.

28. Available at: http://www.encognitive.com/files/Potential%20benefits%20of%20improved% 20protein%20intake%20in%20older%20people.pdf. Accessed June 12, 2013.

29. Nair KS, Short KR. Hormonal and signaling role of branched-chain amino acids. J Nutr. 2005 Jun;135(6 Suppl):1547S-52S.

30. Available at: http://www.cdc.gov/nchs/fastats/lifexpec.htm. Accessed June 12, 2013.

31. Lan-Pidhainy X, Wolever TM. The hypoglycemic effect of fat and protein is not attenuated by insulin resistance. Am J Clin Nutr. 2010 Jan;91(1):98-105.

32. Jakubowicz D, Froy O. Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and type 2 diabetes. J Nutr Biochem. 2013 Jan;24(1):1-5.

33. Hall WL, Millward DJ, Long SJ, Morgan LM. Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite. Br J Nutr. 2003;89:239-48.

34. 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;104:1241-8.

35. Veldhorst MA, Nieuwenhuizen AG, Hochstenbach-Waelen A, et al. Dose-dependent satiating effect of whey relative to casein or soy. Physiol Behav. 2009;96:675-82.

36. Bowen J, Noakes M, Trenerry C, Clifton PM. Energy intake, ghrelin, and cholecystokinin after different carbohydrate and protein preloads in overweight men. J Clin Endocrinol Metab. 2006;91:1477-83.

37. Baer DJ, Stote KS, Paul DR, Harris GK, Rumpler WV, Clevidence BA. Whey protein but not soy protein supplementation alters body weight and composition in free-living overweight and obese adults. J Nutr. 2011;141:1489-94.

38. Dangin M, Boirie Y, Guillet C, Beaufrere B. Influence of the protein digestion rate on protein turnover in young and elderly subjects. J Nutr. 2002 Oct;132(10):3228S-33S.

39. Available at: http://www.usdec.org/files/PDFs/2008Monographs/WeighWeightManagement_English.pdf . Accessed June 13, 2013.

40. Doherty TJ. Invited review: Aging and sarcopenia. J Appl Physiol. 2003. 95(4):1717-27.

41. Graf S, Egert S, Heer M. Effects of whey protein supplements on metabolism: evidence from human intervention studies. Curr Opin Clin Nutr Metab Care. 2011 Nov;14(6):569-80.

42. Paddon-Jones D, Sheffield-Moore M, Katsanos CS, Zhang XJ, Wolfe RR. Differential stimulation of muscle protein synthesis in elderly humans following isocaloric ingestion of amino acids or whey protein. Exp Gerontol. 2006 Feb;41(2):215-9.

43. McKiernan SH, Colman RJ, Lopez M, et al. Caloric restriction delays aging-induced cellular phenotypes in rhesus monkey skeletal muscle. Exp Gerontol. 2011 January;46(1):23-9.

44. Paddon-Jones D, Short KR, Campbell WW, Volpi E, Wolfe RR. Role of dietary protein in the sarcopenia of aging. Am J Clin Nutr. 2008 May;87(5):1562S-6S.

45. Koopman R, Verdijk L, Manders RJ, 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 Sep;84(3):623-32.

46. Dardevet D, Sornet C, Balage M, Grizard J. Stimulation of in vitro rat muscle protein synthesis by leucine decreases with age. J Nutr. 2000 Nov;130(11):2630-5.

47. Katsanos CS, Kobayashi H, Sheffield-Moore M, Aarsland A, Wolfe RR. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006 Aug;291(2):E381-7.

48. Fujita S, Dreyer HC, Drummond MJ, et al. Nutrient signalling in the regulation of human muscle protein synthesis. J Physiol. 2007 Jul 15;582(Pt 2):813-23.

49. Dreyer HC, Drummond MJ, Pennings B, et al. Leucine-enriched essential amino acid and carbohydrate ingestion following resistance exercise enhances mTOR signaling and protein synthesis in human muscle. Am J Physiol Endocrinol Metab. 2008 Feb;294(2):E392-400.

50. Fujita S, Volpi E. Amino acids and muscle loss with aging. J Nutr. 2006 Jan;136(1 Suppl):277S-80S.

51. Morley JE, Thomas DR, Wilson MM. Cachexia: pathophysiology and clinical relevance. Am J Clin Nutr. 2006 Apr;83(4):735-43.

52. Hack V, Schmid D, Breitkreutz R, et al. Cystine levels, cystine flux, and protein catabolism in cancer cachexia, HIV/SIV infection, and senescence. FASEB J. 1997 Jan;11(1):84-92.

53. Dillon EL, Basra G, Horstman AM, et al. Cancer cachexia and anabolic interventions: a case report. J Cachexia Sarcopenia Muscle. 2012 Dec;3(4):253-63.

54. Bounous G, Baruchel S, Falutz J, Gold P. Whey proteins as a food supplement in HIV-seropositive individuals. Clin Invest Med. 1993 Jun;16(3):204-9.

55. Aoe S, Toba Y, Yamamura J, et al. Controlled trial of the effects of milk basic protein (MBP) supplementation on bone metabolism in healthy adult women. Biosci Biotechnol Biochem. 2001;65:913-8.

56. Parodi PW. A role for milk proteins and their peptides in cancer prevention. Curr Pharm Des. 2007;13(8):813-28.

57. McIntosh GH, Regester GO, Le Leu RK, Royle PJ, Smithers GW. Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats. J Nutr. 1995 Apr;125(4):809-16.

58. Tsuda H, Sekine K, Ushida Y, et al. Milk and dairy products in cancer prevention: focus on bovine lactoferrin. Mutat Res. 2000 Apr;462(2-3):227-33.

59. Available at: http://www.cdc.gov/features/vitalsigns/cardiovasculardisease/. Accessed June 14, 2013.

60. Available at: http://usdec.files.cms-plus.com/Publications/CardioHealth_English.pdf. Accessed June 14, 2013.

61. Zhang X, Beynen AC. Lowering effect of dietary milk-whey protein v. casein on plasma and liver cholesterol concentrations in rats. Br J Nutr. 1993 Jul;70(1):139-46.

62. Meltzer CC, Smith G, DeKosky ST, et al. Serotonin in aging, late-life depression, and Alzheimer's disease: the emerging role of functional imaging. Neuropsychopharmacology. 1998 Jun;18(6):407-30.

63. Meltzer CC, Price JC, Mathis CA, et al. Serotonin 1A receptor binding and treatment response in late-life depression. Neuropsychopharmacology. 2004 Dec;29(12):2258-65.

64. Fernstrom JD, Wurtman RJ. Brain serotonin content: physiological dependence on plasma tryptophan levels. Science. 1971;173:149-52.

65. Fernstrom JD, Wurtman RJ. Brain serotonin content: physiological regulation by plasma neutral amino acids. Science. 1972;178:414-6.

66. Markus CR, Olivier B, Panhuysen GE, 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 Jun;71(6): 1536-44.

67. 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 Jun;75(6):1051-6.

68. Camfield DA, Owen L, Scholey AB, Pipingas A, Stough C. Dairy constituents and neurocognitive health in ageing. Br J Nutr. 2011 Jul;106(2):159-74.

69. Chatterton DE, Nguyen DN, Bering SB, Sangild PT. Anti-inflammatory mechanisms of bioactive milk proteins in the intestine of newborns. Int J Biochem Cell Biol. 2013 May 6.

70. Rahman I, MacNee W. Oxidative stress and regulation of glutathione in lung inflammation. Eur Respir J. 2000 Sep;16(3):534-54.

71. Buffinton GD, Doe WF. Depleted mucosal antioxidant defences in inflammatory bowel disease. Free Radic Biol Med. 1995;19:911-8.

72. Duggan C, Stark AR, Auestad N, et al. S. Collier. 2004. Glutamine supplementation in infants with gastrointestinal disease: a randomized, placebo-controlled pilot trial. Nutrition.2004;20:752-6.

73. Walzem RL, Dillard CJ, German JB. Whey components: millennia of evolution create functionalities for mammalian nutrition: What we know and what we may be overlooking. Crit Rev Food Sci Nutr. 2002;42:353-75.

74. Fioramonti J, Theodorou V, Bueno L. Probiotics: what are they? What are their effects on gut physiology? Best Pract Res Clin Gastroenterol. 2003;17:711-24.

75. Teitelbaum JE, Walker WA. Nutritional impact of pre- and probiotics as protective gastrointestinal organisms. Annu Rev Nutr 2002;22:107-38.

76. Matsumoto H, Shimokawa Y, Ushida Y, Toida T, Hayasawa H. New biological function of bovine alpha-lactalbumin: Protective effect against ethanol- and stress-induced gastric mucosal injury in rats. Biosci Biotechnol Biochem. 2001 May;65(5):1104-11.

77. Cross M L, Gill HS. Immunomodulatory properties of milk. Brit J Nutr. 2000;84:S81-9.

78. Clare DA, Swaisgood HE. Bioactive milk peptides: A prospectus. J Dairy Sci. 2000;83:1187-95.

79. Low PPL, Rutherford KJ, Gill HS, Cross ML. Effect of dietary whey protein concentrate on primary and secondary antibody responses in immunized BALB/C mice. Int Immunopharmacol. 2003;3:393-401.

80. Bounous G, Kongshavn PA, Gold P. The immunoenhancing property of dietary whey protein concentrate. Clin Invest Med. 1988 August;11(4):271-8.

81. Bounous G, Papenburg R, Kongshavn PA, Gold P, Fleiszer D. Dietary whey protein inhibits the development of dimethylhydrazine induced malignancy. Clin Invest Med. 1988;11(3)213-7.

82. Ford JT, Wong CW, Colditz IG. Effects of dietary protein types on immune responses and levels of infection with Eimeria vermiformis in mice. Immunol Cell Biol 2001;79(1):23-8.

83. Bounous G, Kongshavn PA. Differential effect of dietary protein type on the B-cell and T-cell immune responses in mice. J Nutr. 1985;115(11):1403-8.

84. McCay CM, Crowel MF. Prolonging the life span. Scientific Monthly. 1934 Nov;39(5):405-14.

85. McCay CM, Crowell MF, Maynard LA. The effect of retarded growth upon the length of life span and upon the ultimate body size. Nutrition. 1935;5:155-71.

86. Ward PP, Paz E, Conneely OM. Multifunctional roles of lactoferrin: a critical overview. Cell Molecul Life Sci. 2005;62,2540-8.

87. Wakabayashi H, Yamauchi K, Takase M. Inhibitory effects of bovine lactoferrin and lactoferricin B on Enterobacter sakazakii. Biocontrol Sci. 2008;13:29-32.

88. Liepke C, Adermann K, Raida M, et al. Human milk provides peptides highly stimulating the growth of bifidobacteria. Eur J Biochem. 2002;269:712-8.

89. Okazaki Y, Kono I, Kuriki TJ, et al. Bovine lactoferrin ameliorates ferric nitrilotriacetate-induced renal oxidative damage in rats. Clin Biochem Nutr. 2012 Sep;51(2):84-90.

90. Raghuveer TS, McGuire EM, Martin SM, et al. Lactoferrin in the preterm infants"' diet attenuates iron-induced oxidation products. Pediatr Res. 2002;52:964-72.

91. Shoji H, Oguchi S, Shinohara K, et al. Effects of iron-unsaturated human lactoferrin on hydrogen peroxide-induced oxidative damage in intestinal epithelial cells. Pediatr Res. 2007;61:89-92.

92. Iigo M, Shimamura M, Matsuda E, et al. Orally administered bovine lactoferrin induces caspase-1 and interleukin-18 in the mouse intestinal mucosa: a possible explanation for inhibition of carcinogenesis and metastasis. Cytokine. 2004;25:36-44.

93. Oguchi S, Walker WA, Sanderson IR. Iron saturation alters the effect of lactoferrin on the proliferation and differentiation of human enterocytes (Caco-2 cells). Biol Neonate. 1995;67:330-9.

94. Spadaro M, Caorsi C, Ceruti P, et al. Lactoferrin, a major defense protein of innate immunity, is a novel maturation factor for human dendritic cells. FASEB J. 2008;22:2747-57.

95. Ashida K, Sasaki H, Suzuki YA, Lonnerdal B. Cellular internalization of lactoferrin in intestinal epithelial cells. Biometals. 2004;17:311-5.

96. Garre C, Bianchi-Scarra G, Sirito M, et al. Lactoferrin binding sites and nuclear localization in K562(S) cells. J Cell Physiol. 1992;153:477-82.

97. Tung YT, Chen HL, Yen CC, et al. Bovine lactoferrin inhibits lung cancer growth through suppression of both inflammation and expression of vascular endothelial growth factor. J Dairy Sci. 2013 Apr;96(4):2095-106.

98. Ono T, Murakoshi M, Suzuki N, et al. Potent anti-obesity effect of enteric-coated lactoferrin: decrease in visceral fat accumulation in Japanese men and women with abdominal obesity after 8-week administration of enteric-coated lactoferrin tablets. Br J Nutr. 2010 Dec;104(11):1688-95.

99. Maher P. Modulation of multiple pathways involved in the maintenance of neuronal function during aging by fisetin. Genes Nutr. 2009 Sep 10.

100. Sadruddin S, Arora R. Resveratrol: biologic and therapeutic implications. J Cardiometab Syndr. 2009 Spring;4(2):102-6.

101. Joseph JA, Fisher DR, Cheng V, Rimando AM, Shukitt-Hale B. Cellular and behavioral effects of stilbene resveratrol analogues: implications for reducing the deleterious effects of aging. J Agric Food Chem. 2008 Nov 26;56(22):10544-51.

102. Salas A, Subirada F, Perez-Enciso M, et al. Plant polyphenol intake alters gene expression in canine leukocytes. J Nutrigenet Nutrigenomics. 2009;2(1):43-52.

103. Ruiz PA, Braune A, Holzlwimmer G, Quintanilla-Fend L, Haller D. Quercetin inhibits TNF-induced NF-kappaB transcription factor recruitment to proinflammatory gene promoters in murine intestinal epithelial cells. J Nutr. 2007 May;137(5):1208-15.

104. Widlansky ME, Duffy SJ, Hamburg NM, et al. Effects of black tea consumption on plasma catechins and markers of oxidative stress and inflammation in patients with coronary artery disease. Free Radic Biol Med. 2005 Feb 15;38(4):499-506.

105. http://www.naturalnews.com/045202_whey_protein_obesity_diabetes_prevention.html

106. http://www.acs.org/content/acs/en/pressroom/presspacs/2014/acs-presspac-april-30-2014/whey-beneficially-affects-diabetes-and-cardiovascular-disease-risk-factors-in-obese-adults.html

107. http://www.diabetes.co.uk/news/2014/may/whey-protein-linked-to-lower-diabetes-risk-in-obese-adults-94407038.html

108. http://www.sciencedaily.com/releases/2013/10/131010091557.htm

109. http://www.sciencedaily.com/releases/2010/12/101208125624.htm

Video transcription

Hi everyone, Mike Stuchiner, Master Herbalist, here with Z Natural Foods. Before we get started on today's video, I need to give you our medical disclaimer. The information you are about to receive is for entertainment and educational purposes only. It is not intended to treat, prescribe, or diagnose any specific or general medical condition and should not be used as a substitute for your primary healthcare provider's diagnosis, treatment plan, or medical information. With that said, if you want more information about me, you can also check out my YouTube channel, "A Master Herbalist's Perspective." But for now, let's move on to today's video. Today, we're going to answer the question, "What does undenatured protein mean?" Well, to correctly answer this question, it's vital to understand what is first meant by denatured protein. Denatured protein is the alteration in the folding patterns of protein by heat or chemical reaction from its original formation. Protein function depends on its structure and shape, and heat causes proteins to vibrate and weaken the bonds that hold their complex shape. When a protein has become denatured, it is no longer considered functional in the same elaborate manner. In simple terms, undenatured proteins are pure, properly functioning proteins without any structural deformation, intact with all bioavailable nutrients and constituents. It is essential to note that we don't tend to use the term "unprocessed" to define an undenatured protein because everything goes through some processing to create an end product. For example, whey protein isolate undergoes a precise filtration process that removes lactose and produces an end product yielding a higher amount of protein per serving with fewer fats and carbohydrates. Because no chemicals and heat were used in this process, the protein bonds were not weakened, so whey protein isolate, in this case, is considered an undenatured protein. Is undenatured protein good for you? When you look at an undenatured protein from a bird's eye view, it's easy to say that any undenatured protein will be better for you than one that has been denatured. But here at Z Natural Foods, we believe there is more to this question than what meets the eye, and it depends on many other factors. Yes, undenatured protein is the purest form, containing all bioactive compounds as nature intended. Undenatured whey protein has a wide range of components like beta-lactoglobulin, alpha-lactalbumin, immunoglobulins, and lactoferrins. This is generally a much better choice, again from a bird's eye view, for all intended purposes. A protein that has become denatured, so through cooking with heat or some other process, is not necessarily bad because, in reality, we eat these forms of protein all the time. For example, a hard-boiled egg is considered a form of denatured protein. The heat used to make a hard-boiled egg changed its structural integrity, but it still has excellent nutritional value and all the amino acids to create a complete protein. Another example is when we cook meat on the grill or microwave our food. These are both considered forms of heat cooking processes that change the protein's structural integrity, yet it does not change the value of being a complete protein. Athletes worldwide who prepare meals ahead of time will often use microwaves to reheat the food. I have a question for you: Do any of those athletes look like they're malnourished or lacking quality protein? I don't think so. What happens when whey protein is denatured? When whey protein becomes denatured, it tends to lose nutrients and compounds that make undenatured whey protein a fantastic food. But understand that undenatured whey is much more than just a protein. It is highly nourishing and provides the body with essential compounds to support and restore well-being. Proteins are complex three-dimensional structures built out of amino acids. The primary cause of why whey protein becomes denatured again is exposure to heat or chemicals that create an unstable protein structure through a process known as unfolding. There are various degrees of process, and your body naturally unfolds proteins through the natural digestive process. As discussed in the questions above, denatured protein is not exactly useless. Some products are actually purposely denatured to create a faster-absorbing form of protein, like what is known as partially denatured hydrolyzed whey protein. When should I take my proteins? Well, there are various theories on this topic, and the answer to this question is quite convoluted and depends on several factors. The first is the form of whey or other milk-based proteins being used. For example, whey isolate, whey concentrate, hydrolyzed whey, or just straight casein. The next is your intended goal, muscle gain, weight loss, blood sugar control, or supporting a healthy immune system response. Whey protein isolate is your choice if you want to help with muscle recovery post-workout because it's an isolated form of protein, which yields a higher amount of protein, allowing for faster absorption. While there are mixed opinions on how quickly one should ingest whey protein or any kind of protein post-workout, consuming it within one hour is usually optimum. Adding a carbohydrate source to your shake to replenish glycogen is also advisable if you are someone who is intaking carbohydrates. If you're creating a post-workout drink, then using a high molecular weight carbohydrate with hydrolyzed whey protein will provide the glycogen and amino acids needed for recovery. To support recovery when you're asleep, drinking whey concentrate or casein is a good choice as these will act as a slower, more time-released source to provide the body with the essential nutrients throughout the night. Because you're getting so many essential nutrients and compounds, high-quality protein, and it is also a source of great fat, whey protein concentrate is ideal for supporting a healthy immune system response and recovery. So, guys, I hope that this answered some very simple questions about proteins that are considered denatured versus undenatured and so on and so forth. Mike Stuchiner, Master Herbalist with Z Natural Foods. See you next time!

Hi everyone, Mike Stuchiner, Master Herbalist here with Z Natural Foods, and today's video is going to be on the topic of what is better: protein concentrate or protein isolate. But before we get started, I do need to mention two things. One, for more information about me, please go to my YouTube channel at, "A Master Herbalist's Perspective." And number two is our health disclaimer, which is: the information you're about to receive is for educational purposes only and is not intended to treat, prescribe, or diagnose any specific or general medical conditions. It is also not intended to be a replacement for your primary healthcare provider's diagnosis, treatment protocol, and medical information. With that said, let's get started. Some of the more popular questions we get at Z Natural Foods are related to the benefits and uses of protein powders. While deciding which source of protein powder is best for you may seem like your top priority, a related topic regarding the differences between a protein concentrate and isolate might actually be more important when attempting to maximize your protein powder benefits. So today, I'm going to answer the question of what is better: a protein concentrate or isolate. As always, I don't just answer your questions. I give you a thorough explanation as to why and provide critical details necessary to understand what you're about to hear. In simple terms, how we define "better" in this specific particular case is relative to the individual's goals, how well that individual utilizes what they consume, and the purpose for using a specific form of protein at a particular time. To answer this question correctly, let's review a few fun facts about proteins and the role they play in the big picture. So let's begin with denatured versus undenatured protein. Denatured protein is the alteration in folding patterns of protein by heat or chemical reaction from its original formation. Protein function depends on its structural shape, and heating causes proteins to vibrate, weakening the bonds that hold this complex shape. Undenatured protein is pure, properly functioning proteins without structural deformation, with all bioavailable nutrients and constituents. It's important to note that we at Z Natural Foods do not use the term "unprocessed" to define undenatured protein because everything goes through some processing to create an end product. For example, whey protein isolate goes through a very precise filtration process, removing the lactose and producing an end product yielding a higher amount of protein. Per serving with less fat and carbohydrates. Undenatured proteins are the purest form containing all bioactive compounds, as nature intended, like beta-lactoglobulin and alpha-lactalbumin, immunoglobulins, and lactoferrin. In a perfectly balanced state, a protein denatured through cooking with heat or some other process is not necessarily a bad thing. For example, a hard-boiled egg is regarded as a form of denatured protein, the heat used to make the hard-boiled egg changes its structural integrity, but overall it's still an excellent nutritional source, and all the amino acids necessary to form a complete protein, essential and non-essential amino acids and protein storage. There are 20 different amino acids that your body needs for various functions. 11 of the 20 are produced by the body, called non-essential amino acids. The other nine, called essential amino acids, we get from food because the body cannot produce them on its own. Proteins are not stored for later use. The body converts excess protein into glucose and triglycerides to supply energy and build energy reserves. When we eat a complete source of protein, the body breaks it down into amino acids to create muscle protein, along with a host of other proteins in the body for what are known as enzymatic reactions. The nine essential amino acids also act as what is known as regulatory signaling molecules. All the body is concerned about is having nine or nine essential amino acids when creating muscle and enzyme proteins. The overall result is the same whether the protein comes from one source, which would be like a concentrate or a combination of sources like plant protein. To be clear, this is not me saying that other factors don't affect the value and utilization of different sources of protein. It's just what I am trying to send out there as a message is, in the bigger picture, our body ultimately really does not know the difference. As long as those amino acids are present in the body, we can do so. The difference between a protein powder concentrate and an isolate is comparing a protein isolate and concentrate comes down to what you gain versus what you lose. As I stated earlier in this video, protein powder concentrates are considered the closest products intended to provide us with a high-quality source of protein with all cofactors and constituents available for a balanced and complete source of nourishment. The term concentrate, though, can be slightly misleading, as it implies that the consumer is getting a quantitatively more significant amount of protein. This is simply not the case. You are getting a more well-rounded end product with a greater spectrum of uses that may benefit overall health. Whey protein isolates, on the other hand, are a more refined product yielding a higher amount of protein with the goal of specific targeted action and application. Generally speaking, whey protein isolate, as an example, is a complete protein yielding approximately 90% protein concentration. It contains no fat and carbohydrates unless some of it is high in branched-chain amino acids, especially leucine. It is considered an undenatured protein. However, if the raw material company uses a filtration process that uses heating components, it may denature the proteins. But components like beta-lactoglobulin, alpha-lactalbumin, and immunoglobulins, and lactoferrin are proteins by definition. Contrary to popular opinion, whey protein isolate does contain these critical factors, just in smaller amounts. Whey isolate may contain tiny amounts of lactose as well. Whey Protein Concentrate is a complete protein yielding approximately 80% protein concentrate, approximately three grams of carbohydrates, and two grams of fat per average serving. Whey Protein concentrate has many other components in fairly high amounts, like as mentioned before, beta-lactoglobulin, alpha-lactalbumin, immunoglobulins, and lactoferrin. It is a quality source of branched-chain amino acids, and it is an undenatured protein. Once again, whey concentrate does contain lactose. Therefore, the difference between isolate and concentrate comes down to the three following ideas: how much protein, carbohydrates, and fat you're getting in the product, the intrinsic details about the conditions under which the product is produced to create the end product, and the individual's specific standards or needs. So this leads me to another area of this video I want to discuss, which is, which is easier to digest, whey isolate or whey concentrate? I stated in previous protein articles I've done that the biological value of protein is one of many markers that determine how well biological value measures how efficiently the body utilizes each source of protein from different foods with a high biological value correlating to an increased supply of essential amino acids. The equation of biological value is calculated from nitrogen used from tissue formation divided by the nitrogen absorbed from food, then multiplied by 100. In simple terms, it's the percentage of nitrogen utilized. Nitrogen is the core component of amino acids, the building blocks of protein, and nucleic acids, the building blocks of genetic material. Whey protein, for example, has a biological value of 104. Generally, each individual's ability to digest whey can vary significantly based on factors like lactose protein concentration, carbohydrate sensitivity, and the effects on blood sugar that comes in. For those who tolerate whey protein well, the isolated version seems easier to digest and more efficient to utilize due to the absence of fat and carbohydrates. Whey concentrate contains a more significant amount of lactose and some fats and carbohydrates. Therefore, some individuals may not be as efficient at utilizing this protein form, especially if they are lactose intolerant. If a protein is producing gas, bloating, and goes right through you within two hours of ingestion, this may not be the best source of protein to optimize your results. Please keep in mind one factor. Many people have incredibly mild or delayed reactions to foods that may not appear as more significant problems for years. Therefore, it would take a lot of work to connect the dots. In the end, if you see a progression of good results, you are certainly on the right track. Picking the best protein source for you is a crucial part of optimizing your health and fitness goals. Each form of protein has its own unique characteristics and can offer various benefits based on an individual's needs and requirements. So, which form of whey protein, concentrate, or isolate is better for muscle gain? The answer to this question is not a matter of which is better for muscle gaining, but more importantly, what is the most appropriate time to use each form of protein in order to maximize your benefits and results? There are various theories on this topic, and the answer to this question is quite convoluted and depends on a few different factors: the form of whey or other milk-based protein powders being used, in other words, whey concentrate, isolate, hydrolyzed whey, or casein, and your goals (intended muscle gain, weight loss, blood sugar control, supporting a healthy immune system). All of these things play a vital role in the overall end results. For example, suppose you want to help with muscle recovery. In that case, that's post-workout because it is isolated from a protein that yields a higher amount of protein and is void of carbohydrates, allowing for faster absorption. While there are mixed opinions about exactly how quickly you should ingest whey post-workout, consuming it within one hour would be optimized. Any carbohydrate source, protein shake, or real grass, and replenish glycogen is often also among the suggestions. Suppose you're creating an intra-workout drink, which means a drink that you consume throughout the workout. In that case, using a high molecular weight carbohydrate like a highly branched cyclic dextrin with a hydrolyzed whey protein will provide the glycogen and amino acids needed for recovery. To support recovery when you're asleep, drinking whey concentrate or a casein protein is a good choice, as those will act slower or more as what some might consider a time-released form of protein to provide the body with essential nourishment throughout the night. Because you are getting so many essential nutrients and compounds, high-quality protein, and a good source of fat, whey concentrate is ideal for supporting a healthy immune system and recovery. In conclusion, whether you're consuming isolate or concentrating on a whey protein, you will provide your body with a wide range of nourishing compounds to support overall well-being. After all these years, it looks like we will Miss Muffet, and the spider that sat down beside her got it right. As you better eat your curds and whey. This is Mike Stuchiner, Master Herbalist with Z Natural Foods. I'll see you next time.

High Quality Protein Isolate

This is my 1st time ordering whey protein isolate from Z Natural Foods. It appears to be quite pure. The last company I dealt with was pretty good, but this one clumps less, mixes easier and has less odor/taste.

High quality protein, annoying subscription

I've tried both the plain and the vanilla flavor whey isolate. The plain is superb. The vanilla is OK... not the best vanilla I've had. Stick with the plain.

One other annoying thing is, when you order on a "subscribe & save" basis, they don't send you any email notice when your next shipment is coming up. They just inform you after they sent it. Which means you often end up with more than you need.