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Cloning and Characterization of an Enantioselective l-Menthyl Benzoate Hydrolase From Acinetobacter Sp. ECU2040

Cloning and Characterization of an Enantioselective l-Menthyl Benzoate Hydrolase From Acinetobacter Sp. ECU2040

Jin-Gang Yin, Guo-Chao Xu, Gao-Wei Zheng, Jian-He Xu

Appl Biochem Biotechnol. 2015 Jun;176(4):1102-13.

PMID: 25930985

Abstract:

A new esterase gene abmbh, encoding a benzoate hydrolase which can enantioselectively hydrolyze l-menthyl benzoate to l-menthol, was recently identified from the genomic library of a soil isolate Acinetobacter sp. ECU2040. The abmbh gene contains a 1080-bp open reading frame encoding a protein of 360 amino acids with a calculated molecular mass of 40.7 kDa. The corresponding enzyme AbMBH was functionally expressed in Escherichia coli BL21 (DE3), purified, and characterized. The AbMBH displayed the maximum activity towards p-nitrophenyl butyrate at 50 °C, and an optimum pH of 8.5. A K M of 2.6 mM and a k cat of 0.26 s(-1) were observed towards dl-menthyl benzoate. The AbMBH exhibited a moderate enantioselectivity (E = 27.5) towards dl-menthyl benzoate. It can also catalyze the enantioselective hydrolysis of a variety of racemic menthyl esters, including dl-menthyl acetate, dl-menthyl chloroacetate, and dl-menthyl butyrate.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP89485	Menthyl acetate		89-48-5	Price

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