Denaturing Necessary for the Cold Processed Whey

One thing occurs to this person when knowing the process of cold processed whey is why there is the concern over denaturing protein in the first place. She understands that to assemble glutathione, the body first needs to denature the whey proteins with stomach acid, and then cleave them into amino acids with enzymes. So, denaturing is a necessary part of the process, and she wonders why it can’t have been done in processing rather than in vivo. The only think she can think of is that the cystine dipeptide needs to be undenatured. She wants to know if it is true.

My answer would be that is exactly incorrect when it comes to glutathione production, although some glutathione production can arise from ample amino acids being present. Your bowel lumen directly absorbs the chief whey components undenatured; they are already absorbable not as individual amino acids, but as peptides, which are made of two or more amino acids and sometimes joined with a mineral.

In this case glutamylcysteine, which is glutamine and cysteine joined together, cystine, which is two cysteines joined together, and cysteinylglytamylcysteine, which is two cysteines and a glutamine, are the important precursors that are directly absorbed from the undenatured whey. These must remain unbroken, undenatured, until they are absorbed into the cells, at which point they then are broken and utilized. If they are broken before hand, they don’t get into the cells where 90% of the glutathione is needed.

Conversely, cysteine, the rate-limiting factor in glutathione production itself, in its free, unbound form is treated by the body as a toxin, produces toxic matabolites, and associated toxic side effects. In its free form its effect on glutathione production is nearly absent. I would recommend getting Jimmy Gutman, M.D.s book Glutathione: Your Body’s Most Powerful Healing Agent as a reference.

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