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Entrapment of Pseudomonas cepacia lipase with peracetylated β-cyclodextrin in sol-gel: application to the kinetic resolution of secondary alcohols

Citation

Ghanem, A and Schurig, V, Entrapment of Pseudomonas cepacia lipase with peracetylated β-cyclodextrin in sol-gel: application to the kinetic resolution of secondary alcohols , Tetrahedron: Asymmetry, 14, (17) pp. 2547-2555. ISSN 0957-4166 (2003) [Refereed Article]


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DOI: doi:10.1016/S0957-4166(03)00550-0

Abstract

Co-lyophilized Pseudomonas cepacia lipase with peracetylated β-cyclodextrin was immobilized by the sol–gel process. The gel-entrapped lipase/cyclodextrin was prepared by the hydrolysis of methyltrimethoxysilane (MTMS) in the presence of the co-lyophilized lipase with peracetylated β-cyclodextrin prepared with different weight ratios (enzyme to CD). This type of enzyme preparation was subsequently used in the kinetic resolution of a set of secondary alcohols using isopropenyl acetate as an innocuous acyl donor in toluene as the organic medium. The resulting chiral alcohols (substrate) and the corresponding acetates (product) were baseline separated in one analysis without derivatization using gas chromatography on a new chiral stationary phase (CSP) Chirasil-β-Dex containing an undecamethylene spacer (C11-Chirasil-Dex).

Item Details

Item Type:Refereed Article
Keywords: efficient heterogeneous biocatalysts, organically modified silicates, enhanced reaction rate, immobilized lipase, transesterification, esterification, hydrolysis, solvents, enzymes,, matrix
Research Division:Chemical Sciences
Research Group:Organic Chemistry
Research Field:Organic Green Chemistry
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Chemical Sciences
Author:Ghanem, A (Dr Ashraf Ghanem)
ID Code:57754
Year Published:2003
Web of Science® Times Cited:24
Deposited By:Austn Centre for Research in Separation Science
Deposited On:2009-08-12
Last Modified:2013-01-22
Downloads:0

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