Chaubey, Asha and Parshad, Rajinder and Gupta, Pankaj and Taneja, Subhash C. and Qazi, Ghulam N. and Rajan, C.R. and Ponrathnam, S. (2009) Arthrobacter sp. lipase immobilization for preparation of enantiopure masked β-amino alcohols. Bioorganic & Medicinal Chemistry, 17 (1). pp. 29-34. ISSN 09680896

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Recent reports on immobilization of lipase from Arthrobacter sp. (ABL, MTCC 5125; IIIM isolate) on insoluble polymers have shown altered properties including stability and enantioselectivity. Present work demonstrates a facile method for the preparation of enantiopure b-amino alcohols by modulation of ABL enzyme properties via immobilization on insoluble as well as soluble supports using entrapment/ covalent binding techniques. Efficacies of immobilized ABL on insoluble supports prepared from tetraethylorthosilicate/ aminopropyltriethoxy silane and soluble supports derived from copolymerization of Nvinyl pyrrolidone-allylglycidyl ether (ANP type)/N-vinyl pyrrolidone-glycidyl methacrylate (GNP type) for kinetic resolution of masked b-amino alcohols have been studied vis-à-vis free ABL enzyme/wet cell biomass. The immobilized lipase on different insoluble/soluble supports has shown 21–110 mg/g protein binding and 30–700 U/g activity for hydrolyzing tributyrin substrate. The findings have shown a significant enhancement in enantioselectivity (ee 99%) vis-à-vis wet cell biomass providing ee 70–90% for resolution of b-amino alcohols.

Item Type: Article
Subjects: Biological Sciences
Depositing User: Mr. Amit Nargotra
Date Deposited: 28 Dec 2011 08:08
Last Modified: 28 Dec 2011 08:08

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