There is much confusion about what denaturization is and how it affects whey protein. Denaturation is the breaking down of protein fractions caused by high heat during processing of the protein, most specifically during the pasteurization process. It is true that denaturization can alter the protein fractions but it will not alter the base amino acids that make up the protein. Our bodies do not use the protein fractions in milk; they break these long-chain fractions down into the individual base amino acids and then rebuild these amino acids into any of thousands of proteins that the body requires. So the fact that denaturing a protein alters or destroys the protein fractions within the milk is true, so what, as long as the amino acids remain intact, the end value to the body remains the same. So why does NutraBio put such an emphasis on manufacturing only non-denatured whey protein? There are other issues to consider. If denaturization alters the protein structure, can this affect the bioavailability of the protein? We know that whey isolate breaks down quickly whereas casein breaks down slower, so we use each for different purposes. If denaturization unknowingly changes their bioavailability characteristics, than our supplementation strategies won’t work. In addition denaturing a protein can destroy beneficial nutrients and enzymes. Acid treatment and high heat are both known catalysts for denaturization and unfortunately we don’t know the affects either has on bioavailability because it has never been studied. The standard used for protein digestibility studies is non-acid treated, pasteurized whey which gives us a foundation on which we can build a sound supplement strategy. Changing protein structures without knowing the end result can impact results for better or worse, but since we don’t know, don’t chance it. So even though, in the end you will get the same amount of aminos with denatured vs. non-denatured whey protein, the factors of bioavailability, and retaining higher nutrient and enzyme levels would make non-denatured protein more valuable. NutraBio’s whey protein isolate, whey protein concentrate, casein and hydrolyzed whey proteins are all non-denatured.

But doesn't the high heat from pasteurization of the milk denature the protein?

Many people argue that all whey proteins are denatured because they come from milk and milk by FDA regulations must be pasteurized. But this is not true, because there are a few different types of pasteurization and not all of them subject the milk to heat levels that cause denaturization. Pasteurization of milk can be done in 3 different levels: Low-Temperature (145 degrees), HTST (high-temp short time. 161 degrees for 30 seconds), and UHT (ultra-high temp. 280 degrees for a few seconds). Much of the milk today uses UHT because it is the quickest for production purposes. The problem is that the ultra-high heat not only kills the bacteria but denatures the protein and destroys nutrients and enzymes. HTST pasteurization still denatures the proteins but to a lesser degree. Low-temperature pasteurization (accepted by the FDA) heats the milk at a lower temperature for a longer period of time, eliminating harmful micro-organisms while leaving valuable enzymes and protein fragments intact. Low-Temp pasteurization takes the longest and is the most expensive process so few dairies do it, but it is the best because it does the least damage and leaves the protein virtually undenatured. NutraBio's whey proteins are pasteurized using the low-heat process, so the protein fragments remain fundamentally intact.