Abstract
Salting process is widely used in the process of meat products, whereas few studies have revealed the digestibility of actomyosin after salting treatment, which is closely related with the nutrition of meat. This work reported effect of salting on the structural change and digestibility of actomyosin before and after heat treatment. Actomyosin in 0.4 M and 0.8 M of NaCl had higher content of disulfide bonds, and actomyosin in 0.4 M NaCl showed the largest particle sizes before and after heat treatment. In addition, actomyosin in 0.6 M and 0.8 M of NaCl was oxidized more severely after heat treatment. Based on peptidomics analysis by using liquid chromatography tandem mass spectrometry (LC-MS/MS), actomyosin in 0.6 M was digested more easily, which was followed by sample in 0.8 M and 0.4 M of NaCl in descending order. The lowest digestibility of actomyosin in 0.4 M NaCl was related with its higher content of disulfide bond and severer aggregation behavior. The lower digestibility of actomyosin in 0.8 M NaCl should be related with the higher content of disulfide bonds and surface oxidation. These results highlight the crucial role of salting process in affecting the digestibility of meat protein.