@article { ISI:000261909800003,
	title = {Arthrobacter sp lipase immobilization for preparation of enantiopure masked beta-amino alcohols},
	journal = {Bioorganic \& Medicinal Chemistry},
	volume = {17},
	number = {1},
	year = {2009},
	month = {JAN},
	pages = {29-34},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>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 beta-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 N-vinyl pyrrolidone-allylglycidyl ether (ANP type)/N-vinyl pyrrolidone-glycidyl methacrylate ( GNP type) for kinetic resolution of masked beta-amino alcohols have been studied vis-a-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-a-vis wet cell biomass providing ee 70-90\% for resolution of beta-amino alcohols. (c) 2008 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Arthrobacter sp lipase, beta-Aminoalcohol, Enantioselectivity, Immobilization, soluble polymer},
	issn = {0968-0896},
	doi = {10.1016/j.bmc.2008.11.023},
	author = {Chaubey, Asha and Parshad, Rajinder and Gupta, Pankaj and Taneja, Subhash C. and Qazi, Ghulam N. and Rajan, C. R. and Ponrathnam, S.}
}
