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

作者：Chaubey Asha; Parshad Rajinder^*; Gupta Pankaj; Taneja Subhash C; Qazi Ghulam N; Rajan C R; Ponrathnam S

来源：Bioorganic & Medicinal Chemistry, 2009, 17(1): 29-34.

DOI：10.1016/j.bmc.2008.11.023

• Arthrobacter sp lipase
• Immobilization
• Soluble polymer
• beta-Aminoalcohol
• Enantioselectivity

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.

• 出版日期2009-1-1