Effect of succinic acid deamidation-induced modification on wheat gluten

Abstract

The effect of succinic acid deamidation-induced modification on wheat gluten was investigated in the present study. The changes of surface hydrophobicity, functional properties, secondary structure, and sensibility of proteolysis of modified samples were determined. The solubility of deamidated proteins increased in the isoelectric region of untreated wheat gluten. The isoelectric point of succinic acid deamidated wheat gluten was shifted to a basic pH and existed in the broad pH regions. Foaming property and molecular flexibility of wheat gluten were improved after the modification. The hydrolysis degree of the hydrolysates in proteolysis with flavorzyme and pancreatin increased after succinic acid deamidation. Moreover, succinic acid deamidation-induced modification resulted in little change in molecular weight and secondary structure of the protein. Thus, succinic acid could facilitate unfolding protein conformation. In addition, it could improve protein-water interactions, surface properties, and sensibility of the proteolysis of the deamidated wheat gluten.