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Arthrobacter sp. lipase immobilization for preparation of enantiopure masked β-amino alcohols

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Title Arthrobacter sp. lipase immobilization for preparation of enantiopure masked β-amino alcohols
 
Creator Chaubey, Asha
Parshad, Rajinder
Gupta, Pankaj
Taneja, Subhash C.
Qazi, Ghulam N.
Rajan, C.R.
Ponrathnam, S.
 
Subject Biological Sciences
 
Description 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.
 
Date 2009
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://iiim.csircentral.net/219/1/10.1016j.bmc.2008.11.023.pdf
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
 
Relation http://dx.doi.org/10.1016/j.bmc.2008.11.023
http://iiim.csircentral.net/219/