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Efficient Kinetic Resolution of (RS)-1-phenylethanol by a Mycelium-Bound Lipase From a Wild-Type Aspergillus Oryzae Strain

Efficient Kinetic Resolution of (RS)-1-phenylethanol by a Mycelium-Bound Lipase From a Wild-Type Aspergillus Oryzae Strain

Hong-De Yan, Zhao Wang, Jun-Qing Qian

Biotechnol Appl Biochem. 2017 Mar;64(2):251-258.

PMID: 26854002

Abstract:

A mycelium-bound lipase from Aspergillus oryzae (AOL) exhibited excellent enantioselectivity for kinetic resolution of (RS)-1-phenylethanol ((RS)-1-PE) in organic solvent. The various reaction parameters affecting the conversion and enantioselectivity were studied, including type of acyl donor, solvent, molar ratio, temperature, enzyme amount, and substrate concentration. The optimum reaction conditions were found to be transesterification with vinyl acetate at 30 °C in methyl tert-butyl ether with a vinyl acetate: (RS)-1-PE molar ratio of 1:1 and an enzyme concentration of 60 g/L. At the optimum reaction conditions, the conversion could reach above 46% with >99% enantiomeric excess of the product, (R)-1-phenylethyl acetate, when the substrate concentration was below 1.4 M. The enzyme displayed an excellent enantioselectivity with an E-value of >200 and a strong tolerance for high substrate concentration of up to 1.8 M. Those results indicated that AOL was a promising biocatalyst in the kinetic resolution of (RS)-1-PE.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1445916	(S)-(−)-1-Phenylethanol		1445-91-6	Price
AP312756744	RS-1		312756-74-4	Price

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