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Improving the Solubility of Sulfolobus shibatae B12 Thermophilic Esterase B12est by Bacillus subtilis 168 Lipase LipA

YANG Gui,LIU Songmei(1.Clinical Laboratory,Zhongnan Hospital,Wuhan University,Wuhan 430071,China;2.Laboratory Center,Zhongnan Hospital,Wuhan University,Wuhan 430071)  
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 thermophilic 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 thermostable and retain more than 60% of its initial activity after incubation at 60℃ for 30 min.
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