Purification and Characterization of the Protease from <i>Staphylococcus xylosus</i> A2 Isolated from Harbin Dry Sausages

Abstract

The protease generated from Staphylococcus (S.) xylosus A2, which was isolated from Harbin dry sausages, was purified and characterized. The molecular weight of the purified protease was approximately 21.5 kDa, and its relative activity reached the highest at pH 6.0 and 50 °C. At pH 4.0–8.0 and temperatures of 20–50 °C, the protease was stable. Its activity was significantly improved by Ca2+ and Zn2+ ions (p S. xylosus A2 protease and its future application in fermented meat products.

Keywords

• <i>Staphylococcus xylosus</i>
• protease
• purification
• characterization
• meat protein