A highly regioselective route to arbutin esters by immobilized lipase from Penicillium expansum

YANG, R.-L., LI, N., LI, R.-F., SMITH, T. J. and ZONG, M.-H. (2010). A highly regioselective route to arbutin esters by immobilized lipase from Penicillium expansum. Bioresource technology, 101 (1), 1-5.

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Link to published version:: 10.1016/j.biortech.2009.07.067

Abstract

Immobilized lipase from Penicillium expansum, a novel and inexpensive enzyme preparation that we immobilized in our laboratory, was an excellent catalyst for highly regioselective acylation of arbutin with fatty acid vinyl esters. For the enzymatic butanoylation of arbutin, under the optimal conditions, initial reaction rate was 75.1 mM/h, and substrate conversion and regioselectivity were greater than 99%. In addition, a variety of 6′-esters of arbutin were prepared with high conversion (>99%) and excellent regioselectivity (>99%). It was found that the enzymatic reaction rate varied widely with different acyl donors, presumably owing to their different interactions with the active site of the lipase. The immobilized lipase from P. expansum displayed highest catalytic activity with medium-length straight-chain acyl donors. Acyl donors bearing a substituent or a conjugate double bond gave reduced reaction rates.

Item Type: Article
Research Institute, Centre or Group: Biomedical Research Centre
Identification Number: 10.1016/j.biortech.2009.07.067
Depositing User: Sarah Ward
Date Deposited: 12 May 2010 09:56
Last Modified: 12 May 2010 09:56
URI: http://shura.shu.ac.uk/id/eprint/1825

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