Myofibrillar proteins' intermolecular interaction weakening and degradation: Are they mainly responsible for the tenderization of meat containing l-arginine, l-lysine, or/and NaCl?

Abstract

This study explored the effects of l-arginine, l-lysine, and NaCl alone and in combination on the tenderness of porcine meat. Arg, Lys, and NaCl alone improved the tenderness, decreased the cooking loss, and increased the myofibrillar fragmentation index (MFI) of porcine meat; Both Arg and Lys cooperated with NaCl to better achieve this effect. Furthermore, Arg/Lys collaborated with NaCl to increase muscle fiber swelling and moisture content of the meat and promoted the extraction of main myofibrillar proteins. FT-IR revealed that Arg, Lys, or NaCl alone or in combination caused changes in protein-water interactions. Western blotting revealed varying degrees of meat protein degradation in all cases, but the results did not well coincide with those of shear force and the MFI. Therefore, the weakening of intermolecular forces between myofibrillar proteins was considered the main reason for meat tenderization under the present study conditions.

Keywords: Intermolecular interaction; Myofibrillar proteins; Protein degradation; Tenderness.