An intracellular esterase from Bacillus cereus catalyzing hydrolysis of 1-chloro-3-(1-napthyloxy)-2-acetoxypropanol

An esterase from Bacillus cereus that hydrolyzes 1-chloro-3-(1-napthyloxy)-2-acetoxypropanol was purified to homogeneity. After purification, the molecular mass of the esterase was determined as 43 kDa by SDS-PAGE, and estimated as 45 kDa using gel filtration, suggesting that the enzyme is a monomer. The optimum pH and temperature for activity of the enzyme were 7.0 and 40 degrees C respectively. The N-terminal sequence was determined. Whole cells of this strain were applied to the resolution of 1-chloro-3-(1-napthyloxy)-2-acetoxypropanol.