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by Lauren Del Turco, CPT
We all know our whey protein is made from milk. But how, exactly, does that milk eventually become our favorite birthday cake-flavored powder?
Here’s how it usually works: Cow’s milk is heated or treated with acid—a.k.a. the cheese-making process—which separates its solid proteins (called the ‘curds’) from its liquid proteins (called the ‘whey’), explains Joe Pilewski, Director of Product Development for NutriForce Nutrition. (Yep, like the nursery rhyme.) The curds, which are made mostly of casein protein, are removed, while the liquid whey goes on to become your go-to protein supp.
That liquid whey is then sprayed onto the inside of a big heated steel drum to dry it. Then the dried whey is filtered to remove lactose, carbs, and fat, Pilewski says. (This is done using insanely fine mesh screens or enzymes that break down certain components.) During the process, some of the proteins are broken down into smaller compounds and even individual amino acids. Then, voila! You have the whey protein isolate powder you know and love.
Related: Exactly What To Eat To Build Muscle
But are there any other perks to processing protein at lower temps? The high heat used in standard whey protein processing can cause some proteins to break down, or ‘denature.’ Most of the long-chain proteins in whey survive the high heat—hence why your average tub still packs a solid dose of the muscle-building macro, according to Brian Tanzer, M.S., manager of scientific affairs for The Vitamin Shoppe. But smaller protein chains—like compounds called immunoglobulins and glycomacropeptides—might be denatured and become useless, he says.
These proteins often get overlooked, but they have some pretty important functions: Immunoglobulins stimulate our immune systems while glycomacropeptides stimulate the production of a hormone called cholecystokinin, which promotes satiety. Because native whey is processed at lower temperatures, these smaller compounds may survive manufacturing, suggests Tanzer. So in theory, a native whey supp could potentially pack more immunoglobulins and glycomacropeptides than a conventional powder—but more testing is needed to support this theory.
We all know our whey protein is made from milk. But how, exactly, does that milk eventually become our favorite birthday cake-flavored powder?
Here’s how it usually works: Cow’s milk is heated or treated with acid—a.k.a. the cheese-making process—which separates its solid proteins (called the ‘curds’) from its liquid proteins (called the ‘whey’), explains Joe Pilewski, Director of Product Development for NutriForce Nutrition. (Yep, like the nursery rhyme.) The curds, which are made mostly of casein protein, are removed, while the liquid whey goes on to become your go-to protein supp.
That liquid whey is then sprayed onto the inside of a big heated steel drum to dry it. Then the dried whey is filtered to remove lactose, carbs, and fat, Pilewski says. (This is done using insanely fine mesh screens or enzymes that break down certain components.) During the process, some of the proteins are broken down into smaller compounds and even individual amino acids. Then, voila! You have the whey protein isolate powder you know and love.
Making ‘Native’
A new whey supplement in town, though, called ‘native whey,’ is made using a different process than your average whey supp. Native whey skips the cheese-making process, and is dried at low temperatures, says Pilewski. The raw milk itself is then filtered. The final result is a protein that’s more intact (closer to its original form), which might have a slightly different amino acid profile than your typical whey isolate, according to a study published in BMC Nutrition.Let’s Talk Benefits
Those BMC Nutrition study authors found that native whey contained more leucine than standard whey protein, giving native a slightly higher total protein concentration. As a result, native whey spiked the participants’ blood levels of leucine more than the regular whey. Because leucine (a branched-chain amino acid) is important for protein synthesis—the process in which we build muscle—having more leucine in your blood theoretically sets you up more favorably for building lean mass, the researchers suggest.Related: Exactly What To Eat To Build Muscle
But are there any other perks to processing protein at lower temps? The high heat used in standard whey protein processing can cause some proteins to break down, or ‘denature.’ Most of the long-chain proteins in whey survive the high heat—hence why your average tub still packs a solid dose of the muscle-building macro, according to Brian Tanzer, M.S., manager of scientific affairs for The Vitamin Shoppe. But smaller protein chains—like compounds called immunoglobulins and glycomacropeptides—might be denatured and become useless, he says.
These proteins often get overlooked, but they have some pretty important functions: Immunoglobulins stimulate our immune systems while glycomacropeptides stimulate the production of a hormone called cholecystokinin, which promotes satiety. Because native whey is processed at lower temperatures, these smaller compounds may survive manufacturing, suggests Tanzer. So in theory, a native whey supp could potentially pack more immunoglobulins and glycomacropeptides than a conventional powder—but more testing is needed to support this theory.