An esterase hydrolyzing phthalate esters has been purified from Micrococcus sp. YGJ1. The enzyme, a monomeric protein (Mr = 56 kDa) with a pI of 4.0, hydrolyzes various aliphatic and aromatic carboxylesters. The medium chain (C3-C4) esters are the most preferred substrates. The enzyme is inhibited by HgCl2 and p-chloromercuribenzoate but not by phenylmethylsulfonyl fluoride.
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Purification and characterization of an esterase hydrolyzing monoalkyl phthalates from Micrococcus sp. YGJ1.
J Biochem
January 2005
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu 501-1193, Japan.
An esterase that specifically hydrolyzes medium-chain (C(3)-C(5)) monoalkyl phthalates was purified from phthalate-grown Micrococcus sp. YGJ1. The enzyme activity was split into two fractions by hydrophobic chromatography on Phenyl Sepharose, and the enzymes were purified to homogeneity from each fraction.
View Article and Find Full Text PDFPurification and characterization of an esterase from Micrococcus sp. YGJ1 hydrolyzing phthalate esters.
Biosci Biotechnol Biochem
July 2001
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Japan.
An esterase hydrolyzing phthalate esters has been purified from Micrococcus sp. YGJ1. The enzyme, a monomeric protein (Mr = 56 kDa) with a pI of 4.
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