Modulating the texture of heat-set gels of phosphorylated walnut protein isolates through Glucono-δ-lactone acidification

The gelation of walnut protein isolates has not been extensively studied, mainly due to their inherent poor dispersity. This study investigated the gelation of alkaline-extracted walnut protein isolates (AWPI) and phosphorylated walnut protein isolates (PWPI) induced by heat treatment with glucono-δ-lactone (GDL) acidification, focusing on the impact of GDL concentrations on microstructure, rheology, and texture of the resulting gels. The PWPI gel exhibited lower hardness but a smoother structure than the AWPI gel. Notably, acidification with GDL (0.6–1.2%) significantly increased the stiffness of PWPI gels, increasing storage modulus and yield stress 10–50 times, while weakening AWPI gels. Varying concentrations of GDL effectively modulated the microstructure of the PWPI gels, leading to the altered texture (from a soft-solid state to a well-self-supporting stiff-solid gel) and water holding capacity (from approximately 46% to 85%). Additionally, hydrophobic interactions and disulfide bonds were identified as the primary forces involved in the gels.