木糖葡萄球菌
蛋白酶
水解物
化学
酶
发酵
蛋白酵素
水解
食品科学
生物化学
分子质量
色谱法
细菌
生物
葡萄球菌
金黄色葡萄球菌
遗传学
作者
Hui Wang,Jianhang Xu,Baohua Kong,Qian Liu,Xiufang Xia,Fangda Sun
出处
期刊:Foods
[MDPI AG]
日期:2022-04-11
卷期号:11 (8): 1094-1094
被引量:6
标识
DOI:10.3390/foods11081094
摘要
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 < 0.05). The Michaelis constant and maximum velocity of the protease were 2.94 mg/mL and 19.45 U/mL·min, respectively. The thermodynamic parameters analysis suggested that the protease showed better catalytic properties at 40 °C. Moreover, the protease could hydrolyze meat proteins, and obtained hydrolysate is non-cytotoxic to the HEK-293 cells. These findings provide a theoretical basis for understanding the enzymatic characterization of S. xylosus A2 protease and its future application in fermented meat products.
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