生物医学工程研究2011，Vol.30Issue(1)：39-42,4.
利用Bacillus subtilis168脂肪酶LipA提高Sulfolobus shibatae B12嗜热酯酶B12est的可溶性
Improving the Solubility of Sulfolobus shibatae B12 Thermophilic Esterase B12est by Bacillus subtilis 168 Lipase LipA
杨桂 1刘松梅2
作者信息
- 1. 武汉大学中南医院检验科,武汉,430071
- 2. 武汉大学中南医院实验中心,武汉,430071
- 折叠
摘要
Abstract
Esterase B12est from thermoacidophilic archaeon Sulfolobus shibatae B12 was cloned and over- expressed in E. coli as an inclusion body form, thereby,fusion the lipase LipA from Bacillus subtilis168 to the N terminal of B12est and the fused enzyme expressed as a soluble form. Results of this study showed that the fusion enzyme reserved the characterization of thennophilic esterase and lipase. The fused enzyme could catalyze p- nitrophenyl (p- NP) esters and triacylglycerides. Even in the high temperature, the fused enzyme still have the catalyze activity, it is highly thenrmostable and retain more than 60％ of its initial activity after incubation at 60℃ for 30 min.关键词
脂肪酶/嗜热酯酶/融合酶/融合表达/催化Key words
Lipase/ Thermophilic esterase/ Fusion enzyme/ Fusion expression/ Catalyze分类
医药卫生引用本文复制引用
杨桂,刘松梅..利用Bacillus subtilis168脂肪酶LipA提高Sulfolobus shibatae B12嗜热酯酶B12est的可溶性[J].生物医学工程研究,2011,30(1):39-42,4.
