Effect of Hydrothermal Cooking Combined with High-Pressure Homogenization and Enzymatic Hydrolysis on the Solubility and Stability of Peanut Protein at Low pH
Jiaxiao Li, Aimin Shi, Hongzhi Liu, Hui Hu, Qiang Wang, Benu Adhikari +2 more
Foods
Abstract
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.
Extracted Claims
4 claims extracted from this paper into the knowledge graph
combined modification decreases surface hydrophobicity of peanut protein
“The improvement of solubility was also confirmed from the decrease in surface hydrophobicity and changes in secondary structure.”
combined modification decreases Turbiscan stability index of modified protein in the acidic solution
“Moreover, the Turbiscan stability index of modified protein in the acidic solution was significantly decreased, indicating its excellent stability in low pH.”
combined modification decreases particle size of peanut protein from 74.82 to 21.74 μm
“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.”