Abstract
Complete deamidation (amide bond hydrolysis) of soy protein and some other food protein was achieved by acid hydrolysis. The amide content of the proteins was determined based on the amount of ammonia generated. When soy protein was treated with commercial proteases, deamidation was found to occur to the free glutamine in the hydrolysates. The deamidation was nonenzymatic and was accelerated by anions such as phosphate and bicarbonate. Ammonia was also generated during the proteolysis from sources other than deamidation. The generation of nonamide ammonia was most likely from enzymatic deamination (cleavage of amino groups) because of the reaction of microorganisms.
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