%0 Journal Article %T Display of Serratia marcesens lipase on surface of Escherichia coli using N-terminal domain of ice nucleation protein
利用冰核蛋白N末端结构域在大肠杆菌表面展示粘质沙雷氏菌脂肪酶 %A TAO Zhan-Hua %A ZHANG Bo %A
陶站华 %A 张搏 %J 微生物学通报 %D 2012 %I %X Objective] We constructed an Escherichia coli strain displaying an active lipase on the cell surface by cell surface engineering and characterized the displayed lipase.Methods] Es-cherichia coli surface display vector of lipase was constructed by fusing sequence encoding the N-terminal domain of ice nucleation protein with Serratia marcesens lipase gene,and the re-combinant vector was transformed into Escherichia coli BL21(DE3).Results] The highest lipase activity was observed when the recombinant cells were induced with 0.05 mmol/L iso-propy-β-D-thiogalactoside(IPTG) and cultured at 25 °C for 16 h.Optimal pH and optimal temperature for cell surface-displayed lipase was 9.0 and 40 °C,respectively.The thermal stability of surface-displayed lipase was improved compared with that of free lipase,and the residual activity was above 90 percent of initial activity after incubated at 40 °C for 1 h.Conclusion] The above results suggest that the bacterial surface display technology offers a promising alternative approach for immobilization of lipases. %K Surface display %K Lipase %K Serratia marcesens %K Escherichia coli
表面展示 %K 脂肪酶 %K 粘质沙雷氏菌 %K 大肠杆菌 %U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=78024727B5F4EF6AA9CA8E605B5FC464&aid=9B2BCA8CA9CB30DF2ADC54EE87EA0D23&yid=99E9153A83D4CB11&vid=7C3A4C1EE6A45749&iid=38B194292C032A66&sid=DB9072192D78AF8A&eid=434C478F331656DD&journal_id=0253-2654&journal_name=微生物学通报&referenced_num=0&reference_num=0