cyco, thanks a bunch for the response!
[quote]cycomiko wrote:
wufwugy wrote:
okay, that’s cool. i would like to know what it means when consumed. in retrospect, i realize that i was being ambiguous because i do not believe that heat doesn’t alter the product. i believe that it doesn’t alter it beyond nutritional value other than in possible minute ways. usually, when the word ‘denatured’ is used in discussion it comes with the implication that it’s deleteriously denatured for human consumption.
i’d like to know if this is true. i’d also like to see proof that shows that micellar casein is better for humans than ‘denatured’ casein.
I have been away to a conference for hte past week so I thought i would reply to this.
there is a big problem taking things completely out of context.
During heating (usually has to be significantly hotter than standard pasterurization and usually under differnetial pH than normal milk - to get more denaturing you increase the heat and alter the ph more) there can be a small amount of denaturing of whey, which allows some of the sulphur residues to bind to sections of the kappa casein section fo the casein micelle (kappa casein is the little hairs). This does not change its nutritional properties, but will change its functional properties within a food system. Casein will denature majorly in the stomach whether the product is ‘raw’ or not.
All digestion involves denaturing. Cooking eggs denatures them, cooking steak denatures it. Worrying about denaturing is missing the forest for the trees.
In terms of the casein micelle being destroyed by any normal processing, its a pile of garbage. All currently available (large scale ones) miceallar casein products in the USA are produced from pasteruized milk, and they generally sit around 97-99% undenatured protien. Milk protein concentrate is similar to micellar casein, the only difference is hte whey is not extracted out of the product, it is also around a similar level fo denaturing. Most wheys are highly digestible and around a similar rate of undenatured proteins, depending on what their end uses are for (some are used as a functional ingredient to improve gelling in a product etc.)
The only concern for denaturing whey proteins is any potential biological activity. But that depends on what you are taking gthe protein as. If its just for protein then its not a worry. if its for the bioactive properties, you are probably paying a fortune for biological properties that are not really backed by an evidence base to do anything (although research in the area is continueing)
Micellar Casein vs other caseins being better? better for what? There is very little research looking at Micellar or native caseins, and even then most are not really looking at comparing casein vs casein.[/quote]
what exactly is " completely out of context" here? the study i posted was done within the temp. ranges of pasteurization, and still fell short of the ranges for ultra-pasteurization.
how are we " missing the forest for the trees"? the concern is not about denaturing per se but about wether the protein remains useable/optimal or not . you know this, but thanks for the insult anyway.
odd that someone who so dismissively called for “evidence” has now posted such a vague thesis without any. still, i’ll give you the benefit of the doubt ; perhaps you’re baiting the trap.
[quote]swivel wrote:
what exactly is " completely out of context" here? the study i posted was done within the temp. ranges of pasteurization, and still fell short of the ranges for ultra-pasteurization.
[/quote]Completely out of context because these things happen at physiological tempertures as well. Ie it can happen inside the mammory gland of the cow. And ever at Ultra pasterurization temps (~120deg C) there is only a small proportion happening.
Wait until somebody spray dries the protein (something like whey or micellar casein within in the grow product) that is far higher than any pasteriuization temperture used within the dairy industry.,
What insult? or are you sensitive?
Missing the forest for hte trees, because you are looking at something that makes an extremely small impact in the big picture. In focussing on this very small process you are looking at the micro, while missing the macro.
If you notice I havent contradicted any of your evidence at all, I have agreed with the fact that whey does bond with casein. Even the information provided in your evidence shows that it is of small impact (you can increase the impact, and many do that to improve the functional properties of hte product).
Are you trying to say your own evidence is not good enough for you?