Adaptive replacement of low-value proteins in surimi gels as exemplified by cold-plasma-precipitated sarcoplasmic proteins: Cross-linking or filling effect?

The potential of cold-plasma-precipitated sarcoplasmic protein (CSP) to co-crosslink with myofibrillar proteins (partially replacing surimi) or to act as a filler (partially replacing water) was systematically evaluated. Within the addition range of 0-2.5%, substituting part of the surimi with CSP diluted the concentration of cross-linkable proteins and the formation of key intermolecular forces. The breaking force dropped from 3.05 N (0%) to 2.04 N (2.5%). When CSP replaced part of the water, it acted as a solid filler, enriching the remaining water to increase the relative protein concentration in the continuous phase, promoting conformational transitions, and strengthening hydrogen bonding and hydrophobic interactions. The breaking force reached a maximum of 4.91 N (2.5%). CSP mainly existed in the form of particles that supported the gel skeleton in surimi gels. Fully exploiting this characteristic is beneficial for promoting the high-quality processing and utilization of CSP in surimi products.