Native Whey Protein Isolate to be released next week!

There is a saying – “A little knowledge is a dangerous thing”. I believe that iveyAg has proven that statement true. In his discussion, iveyAg displays a little bit of knowledge of protein chemistry, the human digestive system, and even a little bit of knowledge about whey protein processing. Hiss knowledge, however, is seriously flawed. I’ll go through his discussion and put my comments right next to iveyAg’s comments.

Originally Posted by iveyAg
i wouldn't have thought that they were worth the money really IMO. Because as soon as you eat the protein, it will be denatured anyway, due to the acid in you stomach, and then cut up by the protease enzymes into its constituent amino acids so that absorption can occur True. Once you eat a protein, the acid in your stomach will cause the protein to denature because of the pH change. The structure of the protein will take on a new shape and this is the very definition of denaturation. On the other hand, if one consumes undenatured proteins, when they come in contact with stomach acid, they fold into predictable, consistent shapes. The protease enzymes discussed by iveyAg are, in many cases, custom designed by the body to digest specific proteins in their specific denatured shapes in the stomach. These enzymes fit into the protein structures like a key and break specific amino acid bonds to yield bioactive peptides that have mainly proven to be anabolic for humans. These specific enzymes are not able to fit into or break off bioactive peptides from proteins that have been denatured prior to eating them because they will not fold into the same shape in stomach acid as undenatured proteins. Denaturation refers to a loss of tertiary structure to a protein molecule, which can occur due to change in pH or temperature, or due to enzyme action. Almost True. Denaturation actually refers to any change in shape of a protein molecule and is caused by enzymes, chemicals, elevated temperatures, and/or pH changes. Please pay attention to what iveyAg and I both agree will cause protein denaturation, it will be important later. Concerning iveyAg’s use of the fancy term tertiary structure – he is trying to use a chemical term to establish himself as a chemistry expert. Don’t be fooled. iveyAg is no chemistry expert. If he was, he would know that protein subunits (example: alpha casein, beta casein, etc) are usually found in their tertiary structure. These subunits, however, then associate together in larger, more complex structures called quaternary structures. Natural proteins are always made up of subunits and will, naturally, form quaternary structures from those subunits. I submit to you that if the quaternary structure of a protein is not there, then the protein has been denatured. Would you rather consume casein in its micellar structure or would you rather consume alpha casein, beta casein, gamma casein, kappa casein. Etc. That’s the difference between tertiary and quaternary structure. Quaternary structure proteins, when digested will yield bioactive peptides. Tertiary structure proteins will only yield amino acids.This should make little or no difference to how easily they are digested Wrong! The structure of a protein in the stomach makes a huge difference in how easily a protein is digested. Consider whey protein for example. Undenatured whey protein is a quaternary structure consisting of subunits, alpha lactalbumin, beta-lactoglobulin, immunoglobulins, lactoferrin, lactoperoxidase, etc. For the purposes of this discussion, we will consider each quaternary structure to be one protein molecule. In the human digestive system, specific enzymes will easily break down the protein chains to more readily absorbed peptides. The peptides will, in many cases, be bioactive – especially the treasured glutamine-cysteine peptides – these are used by the body to make glutathione and are usually in short supply. When a whey protein has been heat denatured (as is usually the case), a cysteine on one of the whey protein quaternary structures will form a new bond (a cross bridged sulfide bond) with another cysteine on another quaternary structure molecule. The new, larger, cross bonded molecules are referred to as aggregates because that’s what they are – aggregated whey proteins. The very act of cross bridging, changes the structure of the quaternary protein and creates a new, much larger protein that the body was not designed to digest. Worse yet, a new peptide is yielded from digestion of the aggregates … the cysteine-cysteine peptide (called cystine). The digestive system will no longer yield the treasured glutamine-cysteine peptide. Everyone knows that the reputation of whey proteins is that they are fast digesting. Much of the reason they digest fast is that an undenatured whey protein is a relatively small molecule and is fast digested by the stomach acid and proteases. Heat denatured whey proteins digest much slower because they are much bigger molecules. Why are they much bigger molecules? Because they have been disulfide bond cross bridged and have become two, three, or four times as big as an undenatured whey protein. Have you ever experienced bloating or gas after eating whey protein? The bloating and gas are simply signs of digestion difficulty. Why do you think many whey proteim marketers add digestive enzymes to their whey protein products? It is an admission on their part that their whey protein is hard to digest. seeing as proteins are absorbed into the bloodstream as amino acids through the wall of the ileum. This is my understanding of it, as a biochemist (student). I too am a biochemist. I would suggest that you keep studying. Anybody who has read very much about protein metabolism will recognize that the human digestive system efficiently absorbs peptides across the intestinal membrane via non-competitive transport systems. The most efficient are the di-peptides (2 amino acids bonded together) and tri-peptides (three amino acids bonded together). Single amino acids are poorly absorbed via a highly competitive uptake system.
But you don't want to start off with denatured protein as the body cannot make use of it as any amino acid content will be damaged in the refining process. I rest my case! iveyAg has now admitted what we have been saying all along – YOU DON’T WANT TO START OFF BY EATING DENATURED PROTEINS.

The two most common whey protein supplements are whey protein concentrate (WPC) and whey protein isolate (WPI). WPC is produced by a process known as ultrafiltration, a low temperature process that uses pressure and a porous membrane to separate the fat and lactose from untreated sweet whey. This produces a product with approximately 78-83% protein, 6-8 % fat and 4-6% lactose. True. This is a valid description of most whey protein concentrate manufacture. But what happened to the whey before it was made into a concentrate? If you will recall, in his first paragraph iveyAg states that proteins are denatured by enzymes, pH changes and temperature. During the cheesemaking process, the whey proteins are subjected to denaturing, elevated temperatures twice (two separate pasteurizations at 72 degrees C – whey proteins start to heat denature at 61 degrees C), an enzyme called rennet or rennin is added to the milk, chemicals are added to the whey (such chemicals are added to make the filtration process go easier by binding calcium that might otherwise plug the filtration membranes), and pH changes (from a starting pH of about 6.6 down to pH 5.2 and then back up to pH 6.3 to 6.9, depending on who is making the whey protein concentrate. Before the manufacturer ever starts to make whey protein concentrate by the gentle, tenderlovingcare process described above by iveyAG, the proteins in the whey have already been denatured. This is like closing the barn door after the horses have gotten out. I do like iveyAg’s use of the term “sweet whey”. It makes the whey sound as if it is the best, doesn’t it? There are two types of cheese whey – sweet whey and acid whey. The terms describe how severe the whey pH was modified during the cheese manufacture. Sweet whey generally has a pH above 5.0 while acid whey has a pH from 4.2 to 5.0. Having tasted many “sweet” wheys over the years, I can tell you that there is nothing sweet about sweet whey.
To produce WPI, WPC is further processed using either cross-flow microfiltration (CFM) or microflitration (MF), both of which further separate whey protein from fat and lactose using high-tech ceramic filters. This produces a WPI comprised of approximately 90% protein, <1% fat and <1% lactose. True again – as far as the processing goes. Microfiltration generally removes fat – not lactose. Nowadays, not everyone uses ceramic filters in MF. Ther are newer technologies. Basically, a protein fraction comparison of whey protein concentrates versus whey protein isolates shows that WPI’s tend to contain more beta-lactoglobulin (the only cow’s milk protein fraction not found in human milk) and less of the bioactive fractions (alpha lactalbumin, immunoglobulins, lactoferring, etc) than do Whey protein Concentrates. In other words, it appears that metabolically valuable protein constituents are lost in going from a WPC to a WPI.

A third process known as Ion-Exchange can also be used to produce WPI, but this method is now considered obsolete due to the effects of the harsh treatments involved, denaturing the native protein fractions. Wrong! Ion exchange of whey proteins is alive and well. It is actually considered to be one of the most gentle whey protein processing techniques – clay resin beads are mixed into cheese whey. The resin beads have a specific ionic charge and they attract the proteins in the whey. The whey proteins attach to the resin beads. The resin beads are then washed thoroughly to remove unwanted fat and lactose etc that may have attached to the beads. The beads are the mixed into fresh water and the ionic nature of the resin is altered so that the whey proteins detach from the beads. The beads are then separated out from the water and you have a whey protein solution. Ion Exchanged Whey Proteins (IEWP) are the most pure on the market with the lowest fat and lactose content. IEWP’s are the only whey protein powders that are truly more than 90% protein as you consume them. The knock against IEWP is that it is not a complete recovery of the whey protein fractions. IEWP tends to have an abnormally high beta-lactoglobulin content and is usually missing the important bioactive fractions like lactoferrin, lactoperoxidase, and immunoglobulins. The bioactive fractions tend to remain attached to the resin beads and are harder to recover. IEWP is still manufactured in the USA and also in New Zealand. IEWP tends to sell for a higher price that WPC or MF WPI because many people desire it for its’ crystal clear water solution and also it’s low viscosity.

The best quality whey proteins are those that are made via a special process involving low-temperature ultrafiltration and spray drying technology. This ensures that the quality of the whey protein is second to none and the amino profile remains high. Hold it! There is no “special” process involving low temperature ultrafiltration and spray drying. These days, just about everyone on the planet uses the same technique and it is low temperature processing – they have found out over the years that filtration proceeds easier at lower temperatures – less calcium blinding, etc. Again, I have the same question – is the filtration technique that valuable when the whey proteins have already been denatured during the cheese making process? Closing the barn door after the horses escaped?

I need to ask. Why is iveyAg so focused on amino acids? If all you eat proteins for is the amino acids, then don’t even waste your money purchasing whey proteins. Eat the cheaper proteins – soy, rice, wheat, beans. They’ll give you sufficient amino acids. Most of us, however, consume protein supplements for their bioactive properties immune support, anabolic triggers, etc. I will concede that even denatured proteins will supply amino acids. The key, though, is will the protein trigger anabolic functions in your body and will the protein help you to maintain your hard earned lean tissue through prevention of catabolic states (such as illness)? Get your focus off of amino acids! Start thinking about a real competitive edge! Think bioactivity.
In short there are undenatured whey proteins available at low cost without resorting to pro-peptide.
In short, if a whey protein has been manufactured from cheese whey, it has been denatured (by every definition of denaturation – even iveyAg’s definition)! I only know of one truly undenatured whey protein and that is the whey protein in ProPeptide. It is manufactured directly from skim milk and not from cheese whey. If iveyAg really thinks that there are undenatured whey proteins out there at a lower cost than ProPeptide, then please, iveyAg, give us those brand names. We would love to find other sources.
By Phil Connolly

I didn't see any reference to the source of the milk from the Native Whey Protein. Is it sourced from Grass Fed Cows as well? What region do the cows come from?
Thank you!

Instead of "Native Whey" don't you just refer to it as Prolacta from Lactalis? This might help with answering questions about the product. I like to keep things simple. Of course I ordered a 5lb bag, anyway.

Interesting thread - I really love Native Whey. One concern I have, though, is that there must apparently be some signficant heating & denaturing of the product. If you look at the Amino profile, it lists Cystine rather than Cysteine. As far as I know, Gluthione synthesis requires Cysteine. Where am I going wrong?

Of course as all dairy must be pasteurized. Cystine is reduced when digested into two cysteine molecules.

Originally Posted by AlexRogers

Of course as all dairy must be pasteurized. Cystine is reduced when digested into two cysteine molecules.

Thanks - does that mean I AM getting cysteine via native whey, and thereby allowing for Gluthione synthesis?

Originally Posted by Katzenjammer

Thanks - does that mean I AM getting cysteine via native whey, and thereby allowing for Gluthione synthesis?

Of course...native whey is great stuff.

What is the story with the native whey? I bought a 5 lb bag maybe two months ago and the consistency was sort of a clumpy moist powder like Membrane micellar but it mixed well. The latest bag came and it is fine granules like table sugar. A couple shakes in a shaker bottle and I'm getting an inch of foam on top and small chunks stuck to the sides of the bottle. This new bag reminds me of the first batch I got earlier last year and then read there was a switch?? Did PF switch again? I just never know if this is the same stuff or there was a mistake??