Deamidation During Treatment of Soy Protein with Protease

摘要

ABSTRACTWhen soy protein was treated with protease in phosphate buffer, ammonia was generated in addition to the occurrence of peptide bond hydrolysis. The source of the ammonia was likely the nonenzymatic deamidation of glutamine in the hydrolysate because free glutamine was found to deamidate in phosphate buffer with or without protease. Both the glutamine deamidation and the deamidation during enzymatic proteolysis of soy protein were catalyzed by certain anions. Of the anions investigated, phosphate and bicarbonate were by far the most effective in that regard, borate only slightly effective, and acetate not effective at all.