Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2.

Effects of partial substitution of NaCl with KCl, MgCl2 or CaCl2 on oxidative characteristics of myofibrillar protein (MP) in a hydroxyl radical generating system and their heat-induced gel properties were investigated. Results indicated that MP oxidation is dependent upon the different chloride salt types and substitution degree. MP at 0.60 M NaCl was beneficial to protein unfolding and gel quality in the oxidative system. Increased formation of disulfide bonds affected the MP conformation and resulted in a large particle size and an aggregatednetworkofgel at the 50% substitution degree of KCl. The presence of CaCl2 or MgCl2 substitutes contributed to protein polymerization and insolubility. MP aggregation restrained the formation of dense and continuous gel networks during heating, and thus resulted in a low-grade gel. Ca2+ had more serious impact on gel properties than Mg2+, dependent on different cation effects. Substitution of 25% NaCl by KCl gave acceptable gel quality in MP.