Purification and characterization of an esterase from Micrococcus sp YGJ1 hydrolyzing phthalate esters

An esterase hydrolyzing phthalate esters has been purified from Micrococcus sp. YGJ1. The enzyme, a monomeric protein (M-r=56 kDa) with a pl of 4.0, hydrolyzes various aliphatic and aromatic carboxylesters. The medium chain (C-3-C-4) esters are the most preferred substrates. The enzyme is inhibited by HgCl2 and p-chloromercuribenzoate but not by phenylmethylsulfonyl fluoride.