Discovery of an Escherichia coli esterase with high activity and enantioselectivity toward 1,2-O-isopropylideneglycerol esters.

ABSTRACT: Escherichia coli has been widely used as an expression host for the identification of desired biocatalysts through screening or selection assays. We have previously used E. coli in growth selection and screening assays for identification of Bacillus subtilis lipase variants (located in the periplasm) with improved activity and enantioselectivity toward 1,2-O-isopropylideneglycerol (IPG) esters. In the course of these studies, we discovered that E. coli itself exhibits significant cytoplasmic esterase activity toward IPG esters. In order to identify the enzyme (or enzymes) responsible for this esterase activity, we analyzed eight E. coli knockout strains, in which single esterase genes were deleted, for their ability to hydrolyze IPG butyrate. This approach led to the identification of este

SUBMITTER: Godinho LF 

PROVIDER: S-EPMC3165400 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature