摘要
采用盐析、DEAE阴离子交换层析、凝胶层析等步骤,从地衣芽孢杆菌(B·licheniformis)2709的发酵液中获得了电泳纯的碱性蛋白酶。结果发现:提纯酶的活力达61069U/mg,纯化倍数:38.7,活性回收率:19.3%,去酰氨度:20.9%.并研究了该酶的基本酶学特性,碱性蛋白酶最适反应温度为50℃,最适作用pH为10.0。40℃保温2h后该酶保持80%以上的活力,在pH8～11之间有较高的pH稳定性。
The alkaline pmtease was purified from B.licheniformis 2709 by alcohol precipitation, ammonium sulphate precipitation, DEAE ion exchange chromatography, and gel layer chromatography and the purified alkaline was demonstrated to be electmphoretic by SDS-PAGE. The restdts indicated that the enzyme activity of purified protease was 61069 U·mg^-1 with final purification factor, activity recovery factor and deamidation reate of 38.7, 19.3%, and 20.9%, respectively. The optimal conditions for the highest activity of alkaline protease were as follows： pH 10.0, and temperature 50℃. After incubation at 40℃ for 2h, the residual activity of the enzyrne was above 80%, and the enzyme was relatively stable at pH 8-11.
出处
《现代食品科技》
EI
CAS
2010年第2期129-132,148,共5页
Modern Food Science and Technology
基金
国家科技部863课题(2006AA10Z329)
黑龙江省研究生创新科研项目(YJSCX2009-196HLJ)
关键词
碱性蛋白酶
提纯
去酰氨
性质
alkaline protease
pulificafion, deamidation
properties
