Hey everyone - I hope someone here hear can answer this 2 part question for me :-)
1) How does the gluten protein survive high heat surfaces such as the grill?
From what i understand, a protein's activity is based on their structural conformation and most proteins have a narrow range of temperature in which they can maintain their structural integrity before they unravel or denature. A denatured protein loses it's original function.
For example, if I took biologically hazardous Protein A and transformed it into Protein Z through some method of denaturation, protein Z should be harmless.
Here goes Question 2:
MSG: Mono Sodium Glutamate, in terms of chemistry, is the basic form of the amino acid Glutamic Acid. It's also connected to a multitude of neurodegenerative diseases.
When we ingest food, our stomach pumps out concentrated hydrochloric acid which is an extremely strong acid. Theoretically the MSG should be converted back to it's glutamic acid form under these conditions. So I guess my question is:
2) Is it MSG or glutamic acid the culprit?
I don't think MSG is a problem except for the fact it induces overeating through hyperpalatibility. We have discussed the odious Dr. Blaylock here before, who peddles fringe alarmism and supplements to fix the alarmist issues. Needless to say, his ideas are fringe and no study has found a negative effect on MSG in humans. I suspect people who say they are sensitive are actually sensitive to other ingredients in the industrial foods that MSG is used in.
For gluten, there is evidence that heat treatment increases reactivity " It indicated that the gluten obtained by heat treatment exhibited higher reactivity during the polymerization catalyzed by TGase, compared with the original gluten. Submitting to heating resulted in change in molecular flexibility of wheat gluten proteins (Hargreves, Popineau, Meste, & Hemminga (1995) J. Hargreves, Y. Popineau, M.L. Meste and M.A. Hemminga, Molecular flexibility in wheat gluten proteins submitted to heating, FEBS Letters 372 (1995), pp. 103–107.Hargreves, Popineau, Meste, & Hemminga, 1995). The change in molecular flexibility is probably favorable for protein-gel formation." Gliadins and glutenin are very heat resistant anyway, that's why they are so valuable in baking. And either way, denatured proteins very much can have negative effects. Protein Z might not be harmless at all and might actually be worse.
Our stomach does not "pump out concentrated hydrochloric acid", it secretes very dilute hydrochloric acid, about 0.5% concetration. Yes that is 200 times more dilute than concentrated (100%) hydrochloric. So one cannot assume that all the reactions possible with concentrated HCL are possible in our dilute stomach acid. Some reactions need the full concentration acid.
About gluten, I am still experimenting but I have found that cake (baked about 200C presumably) has no effect on me whereas beer and thin wheat wafers do. The heat required to denature gluten completely is apparently just over the melting point of lead, 340C.
I was curious about this too and here's some of what I found...
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