No abstract

BACKGROUND Soybean protein isolate hydrolysates (SPIHs) produced at high hydrostatic pressure have higher bioactivity. The aim of the study was to analyze the effects of different SPIH concentrations obtained under various pressures (0.1, 100, 200, and 300 MPa) on gelling properties, structural characteristics, and main forces of myofibrillar protein (MP) in MP‐SPIH plural gels. RESULTS The MP‐SPIH plural gel with 3% SPIH produced under 200 MPa had the maximum gel strength (0.42 N) and water holding capacity (53.69%). A decline in thermal stability and a rise in storage modulus (G′) of MP‐SPIH plural gels were found with increased SPIH pressure and concentration. Additionally, the addition of SPIHs increased the amounts of α‐helix and β‐sheet, decreased random coil structural content of MP in MP‐SPIH plural gels, and facilitated the generation of a denser and uniform gels network. The molecular forces in MP‐SPIH plural gels were mainly hydrophobic interaction and hydrogen bond. CONCLUSION This study showed that the interaction of MP with 3% SPIH obtained at 200 MPa improved the quality of plural gels. © 2022 Society of Chemical Industry.