Arthrobacter sp. lipase immobilization for preparation of enantiopure masked beta-amino alcohols.
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-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 beta-amino alcohols.
Chaubey
Asha
A
Indian Institute of Integrative Medicine, Canal Road, Jammu Tawi 180001, India.
Parshad
Rajinder
R
Gupta
Pankaj
P
Taneja
Subhash C
SC
Qazi
Ghulam N
GN
Rajan
C R
CR
Ponrathnam
S
S
D000605:Amino Alcohols / Q000138:chemical synthesis*; D001173:Arthrobacter / Q000201:enzymology*; D018533:Biomass; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006868:Hydrolysis; D008049:Lipase / Q000378:metabolism*; D008722:Methods; D013237:Stereoisomerism; D014280:Triglycerides
D000605:Amino Alcohols; D004800:Enzymes, Immobilized; D014280:Triglycerides; D008049:Lipase; C005830:tributyrin