Purification and Properties of Carboxylesterase from Ochrobactrum anthropi

抄録

Carboxylesterase from Ochrobactrum anthropi was purified to homogeneity by a combination of DEAE-cellulose, Sephadex G-100, and bydroxyapatite column Chromatographies. The molecular weight of the enzyme was calculated to be 58, 000 by Sephadex G-75 gel filtration. SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of two identical subunits with a molecular weight of 30, 000. The enzyme was inactivated by several organophosphates and sulfhydryl reagents. The esterase hydrolyzed only acetate and propionate esters. In the presence of Triton X-100, the esterase hydrolyzed l-menthyl acetate but not its optical isomer. This result suggests that the enzyme can be used for the optical resolution of l-menthol.