Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Guseong-dong, Daejeon 305-701, Republic of Korea.
J Biotechnol. 2010 Apr 1;146(3):126-9. doi: 10.1016/j.jbiotec.2010.01.022. Epub 2010 Feb 6.
Functional expression of the industrially important Pseudomonas and Burkholderia lipases, such as those from P. aeruginosa, B. cepacia and P. fluorescens, was achieved on the cell surface of Escherichia coli using the C-terminal translocator moiety (EstATu) of autotransporter protein (EstA) from P. putida. In particular, lipases which required a lipase-specific foldase (Lif) for their proper folding were for the first time displayed in the active form by coexpression of the Lif protein.
采用恶臭假单胞菌（Pseudomonas putida）自转运蛋白（EstA）的 C 端转运子（EstATu），在大肠杆菌的细胞表面实现了工业上重要的假单胞菌（Pseudomonas）和伯克霍尔德菌（Burkholderia）脂肪酶（如来自铜绿假单胞菌（P. aeruginosa）、洋葱伯克霍尔德菌（B. cepacia）和荧光假单胞菌（P. fluorescens）的脂肪酶）的功能表达。特别是，对于那些需要脂肪酶特异性折叠酶（Lif）才能正确折叠的脂肪酶，首次通过共表达 Lif 蛋白以活性形式进行展示。
