一种盐螺旋菌耐盐耐碱蛋白酶的分离纯化及性质研究  

Purification and characterization of a salt and alkali tolerant protease from Salinispirillum marinum

作　　者：闫函 许真真 李静[1] 刘建国 YAN Han;XU Zhenzhen;LI Jing;LIU Jianguo(College of Chemical Engineering, China University of Petroleum, Qingdao, Shandong 266580, China)

机构地区：[1]中国石油大学(华东)化学工程学院,山东青岛266580

出　　处：《山东科技大学学报（自然科学版）》2021年第6期37-42,共6页Journal of Shandong University of Science and Technology(Natural Science)

基　　金：国家自然科学基金项目(21473256)。

摘　　要：耐盐耐碱蛋白酶是目前高盐食品加工行业最紧缺的酶类,而嗜盐嗜碱菌是筛选此类蛋白酶较为理想的来源。本研究采用硫酸铵沉淀法和凝胶过滤层析法对碱湖来源盐螺旋菌分泌的蛋白酶进行分离纯化,并对其性质进行表征。结果表明,经分离提纯后,蛋白酶的纯度为98.6%,比酶活为3962.2 U/mg。该蛋白酶的最适反应条件为50℃和pH 9.0,且该酶在30~90℃、pH 7.0~13.0范围内能保持70%以上的活性。此外,该蛋白酶在4.0 M氯化钠溶液中能保持90%的活性。有机溶剂二甲基甲酰胺、苯、甲醇、乙醇、丙酮和正己烷对该酶的活性有促进作用或无影响。这是对盐螺旋菌来源蛋白酶的首次报道。Salt and alkali tolerant protease is the scarcest enzyme in high-salt food processing industry,and haloalkaliphilic bacteria is an ideal source for screening the protease.In this paper,the protease secreted by Salinispirillum marinum from Alkali Lake was first purified by ammonium sulfate precipitation and gel filtration chromatography,and its properties were then characterized.The results showed that the purity of the protease was 98.6%and the specific enzyme activity was 3962.2 U/mg.The optimum reaction condition of the protease was 50℃and pH 9.0.It could keep more than 70%of its activity in the range of 30~90℃and pH 7.0~13.0.In addition,the protease could maintain 90%of its activity in 4.0 M NaCl solution.Organic solvents,such as dimethylformamide,benzene,methanol,ethanol,acetone and n-hexane,could promote or did not affect the enzyme activity of the protease.This is the first report of the protease from genus Salinispirillum.

关 键 词：螺旋菌 蛋白酶 分离纯化 酶活 

分 类 号：Q936[生物学—微生物学]