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Old 12-14-2007, 07:45 AM
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Default Dispelling the cooked protein myth - denaturing is irrelevent

Probably one of the most asked questions I have seen is if cooking your proteins a certain way will render them worthless. After doing research over here in Champaign IL, I can say no, it won't.

In our lab, we literally replicate the human digestion process; and often use even harsher conditions.

Proteins have the ability to form 3d structures through covalent and non-covalent attractions; these are secondary and tertiary structures (single peptide chain structures), and quaternary structures (interactions between more than one peptide chain).

When protein enters the body, one of the first steps is the destruction of these 3d structures by pepsin. This is called denaturing. Then trypsin and HCL work to hydrolyze the the proteins into amino acids and di/tri-peptides which are absorbed by Pept 1 + individual amino transports, and the sodium potassium pump.

The key point here is that all cooking your food is going to do is denature your proteins, and hydrolyze them into peptides / aminos. This will only assist in digestion!

Let me just give you one step in our lab that should alleviate your concern: to completely hydrolyze the proteins into amino acids, we place our samples in 6 N of HCL and incubate them in an oven at 100 C for 24 hours! And they are still stable. You know why we use 6 N of HCL? Because that is what the body uses!

Now go eat some denatured protein! [img]/forum/images/graemlins/tongue.gif[/img]
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Gabriel "Venom" Wilson, Ph.D. Nutritional Sciences
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