Improvement of Gelation Properties of Mutton Myofibrillar Protein Using Pea Protein Isolate: Intermolecular Interactions and Rheological Behavior

ABSTRACT This study investigated the regulatory effect of pea protein isolate (PPI) on the physicochemical and gel properties of mutton myofibrillar protein (MP) under heat‐induced conditions. The results showed that the addition of 1%–5% PPI effectively regulated the solubility, surface hydrophobicity, and sulfhydryl content of mutton MP. PPI strengthened the cross‐linking and aggregation of MP molecules through hydrophobic interactions and disulfide bonds, reconstructed the microscopic structure of the protein gel network, significantly improved the water‐holding capacity and mechanical properties of the gel, and reduced cooking loss. This study clarified the mechanism by which PPI improves the gel quality of mutton MP. Without deteriorating gel quality, it provides a novel theoretical basis and technical support for the formulation optimization and industrial development of high‐quality mutton gel products.