Differences in pork myosin solubility and structure with various chloride salts and their property of pork gel

Abstract

The solubility and structure of myosin and the properties of pork gel with NaCl, KCl, CaCl2, and MgCl2 were investigated. Myofibrillar proteins (MPs) with phosphate were more solubilized with NaCl than with KCl (p < 0.05). CaCl2 and MgCl2 showed lower MP solubilities than those of NaCl and KCl (p < 0.05). The α-helix content of myosin was lower in KCl, CaCl2, and MgCl2 than in NaCl (p < 0.05). The pH of pork batter decreased in the order of KCl, NaCl, MgCl2, and CaCl2 (p < 0.05). The cooking yield of the pork gel manufactured with monovalent salts was higher than that of the pork gel manufactured with divalent salts (p < 0.05). The pork gel manufactured with KCl and MgCl2 showed lower hardness than that of the pork gel manufactured with NaCl. The solubility and structure of myosin were different with the different chloride salts and those led the different quality properties of pork gel. Therefore, the results of this study can be helpful for understanding the quality properties of low-slat meat products manufactured by replacing sodium chloride with different chloride salts.

Keywords

• Chloride salt
• Myosin
• Secondary structure
• Gel quality