02108nas a2200277 4500008004100000022001400041245011100055210006900166260008700235300001200322490000700334520109400341653002701435653002301462653001901485653002301504653002301527653002001550100001801570700002201588700002401610700003001634700002101664700002501685856012001710 2012 eng d a0883-911500aImmobilization of enantioselective lipase on soluble supports for kinetic resolution of drug intermediates0 aImmobilization of enantioselective lipase on soluble supports fo a1 OLIVERS YARD, 55 CITY ROAD, LONDON EC1Y 1SP, ENGLANDbSAGE PUBLICATIONS LTDcSEP a499-5090 v273 a
The microbial lipase, Arthrobacter sp. lipase (MTCC 5125), from the Indian Institute of Integrative Medicine repository, is known as an effective catalyst for high enantioselective kinetic resolution of drug intermediates. The ABL was immobilized on water-soluble linear supports by covalently binding it to the epoxy groups on the N-vinyl pyrrolidone/allyl glycidyl ether and N-vinyl pyrrolidone/glycidyl methacrylate copolymers. The immobilized lipase, on different soluble supports, had 90-110 mg/g protein binding and 500-700 U/g hydrolysis activities for tributyrin substrate. These copolymers had soluble/insoluble characteristics in different pH ranges, which is an advantage over insoluble copolymers. A soluble polymer at neutral pH provided better accessibility to the immobilized enzyme, which was recovered by precipitation at pH 2-3 for reuse. Kinetic resolution of racemic acyl derivatives of chiral auxiliaries and drug intermediates, namely, phenyl ethanol, aminoalcohol, and fluoxetine intermediate resulted in a significant enhancement in enantioselectivity (99%).
10aArthrobacter sp lipase10aEnantioselectivity10aImmobilization10aKinetic resolution10aN-vinylpyrrolidone10asoluble polymer1 aChaubey, Asha1 aParshad, Rajinder1 aTaneja, Subhash, C.1 aDeokar, Sarika, Babasaheb1 aRaman, Rajan, C.1 aPonrathnam, Surendra uhttp://library.ncl.res.in/content/immobilization-enantioselective-lipase-soluble-supports-kinetic-resolution-drug-0