Purification and characterization of a novel esterase promising for the production of useful compounds from Microbacterium sp 7-1W

A novel esterase catalyzing regioselective hydrolysis was purified from the membrane fraction of Microbacterium sp. 7-1W, and characterized. The enzyme was solubilized with Brij 58 and purified 13.8-fold to apparent homogeneity with 2.58% overall recovery. The relative molecular mass of the native enzyme as estimated by gel filtration was more than 600000 Da, and the subunit molecular mass was 62000 Da. The enzyme catalyzed cleavage of the terminal ester bonds of cetraxate esters and pantothenate esters. The K-m and V-max values for methyl cetraxate were 0.380 mM and 7.76 mumole min(-1) mg(-1) protein, respectively. The enzyme was inhibited by serine hydrolase inhibitors. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.