摘要
枯草芽孢杆菌(Bacillus Subtilis)B135工程菌能产生抗氧化型碱性蛋白酶,粗酶经硫酸铵分级沉淀,CM-52层析,Sephadex G-100层析,得到凝胶电泳均一样品,比活达到1700U/mg,是粗酶比活的7.69倍.该酶在60℃时酶活力最高,最适pH为10.2,在50℃时,温浴10min后,酶活降低到原来的50%.该酶受1M H_2O_2作用20min后。
Crude oxidatively resistant subtilisin was obtained from culture supernatant of Bacillus subtilis B135, and was purified by ammonium sulfate fractjonation, cellulose CM-52 chromatography and Sephadex G-l00 gel filtration. The purified oxidatively resistant subtilisin was identified to be homogeneous by SDS electrophoresis. The specific activity of purified enzyme was 1700u/mg,7.69-fold of the crude enzyme. The maximum activity was at 60℃ and pH 10.2, After 10 min at 50℃, enzyme activity was 50% of its original activity. The activity of purified enzyme was 96% of its original activity after 20 minutes' exposure to 1M HαOα.
出处
《工业微生物》
CSCD
北大核心
1996年第3期10-14,共5页
Industrial Microbiology
基金
863计划
