In the last paleodigest, Jenny writes:

"Dear Loren,,

Thanks for your well-documented facts about amylase inhibitors.  My
understanding is that these are all very heat labile and denatured by
cooking.  If we eat raw starch we get a bad pain in the belly because
raw starch per
se is resistant to digestion.

Best wishes  Jennie".

        Both alpha amylase inhibitors (in cereals and legumes) and trypsin
inhibitors (primarily in legumes) are not fully denatured by normal
cooking processes.    It is reported, "Protein alpha amylase inhibitors
may represent as much as 1% of wheat flour and, because of their
thermostability, they persist through bread baking being found in large
amounts in the center of loaves." (Buonocore V. et al.  Wheat protein
inhibitors of alpha amylase.  Phytochemistry 1977;16:811-20).   Further
in his treatise on antinutrients, Liener states, "However because of the
necessity of achieving a balance between the amount of heat necessary to
destroy the trypsin inhibitors and that which may result in damage to
the nutritional or functional properties of the protein, most
commercially available edible grade soybean products retain 5 to 20% of
the trypsin inhibitor activity originally present in the raw soybeans
from which they were prepared." (Liener IE.  Implications of
antinutritional components in soybean foods.  Crit Rev Food Sci Nutr
1994;34:31-67.).

                                Cordially,

                                Loren