LAUSR

A novel method combining high-pressure homogenization with enzymatic hydrolysis and hydrothermal cooking (HTC) was applied in this study to modify the structure of peanut protein, thus improving its physicochemical properties. Results showed that after combined modification, the solubility of peanut protein at a pH range of 2–10 was significantly improved. Moreover, the Turbiscan stability index of modified protein in the acidic solution was significantly decreased, indicating its excellent stability in low pH. From SDS-PAGE (Sodium Dodecyl Sulfate PolyAcrylamide Gel Electrophoresis), the high molecular weight fractions in modified protein were dissociated and the low molecular weight fractions increased. The combined modification decreased the particle size of peanut protein from 74.82 to 21.74 μm and shifted the isoelectric point to a lower pH. The improvement of solubility was also confirmed from the decrease in surface hydrophobicity and changes in secondary structure. This study provides some references on the modification of plant protein as well as addresses the possibility of applying peanut protein to acidic beverages.