03050nas a2200289   4500008004100000022001400041245012900055210006900184260009900253300001200352490000700364520194100371653004402312653002202356653002902378653004002407653001902447653001102466100001802477700002202495700002202517700002402539700001802563700002602581700002402607856012902631       2008                        eng d  a1359-511300aLipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates0 aLipase enzyme immobilization on synthetic beaded macroporous cop  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcAPR  a321-3300 v433 a<p>Lipase isolated from Arthrobacter sp. (bacterial strain, MTCC No. 5125) at RRL Jammu, being used for various process development. Arthrobacter sp. lipase (ABL) now has been immobilized on synthetic polymers and reused many a times. In this investigation number of various synthetic macroporous alkylated glycidyl epoxy copolymers with varying hydrophobicity, pore volume and surface area were prepared and used for this study. Among all the polymers prepared and used only two epoxy polymers GMA-EGDM 75-20(I) and GMA-EGDM 75-30(I) with particle size in the range of 150-450 nm, epoxy groups 80 and 70%, tertiary amino groups 20 and 30% was found suitable for immobilization of lipase (ABL). Dibutyl amine (DBA) incorporation created an internal pore radii 20-50 nm and hydrophobic microenvironment in both the polymers for binding the enzyme, which led to improvement in stability and enatioselectivity in racemic resolution process especially by binding to one of the isomers. The optimal ABL binding capacity of polymer GMA-EGDM 75-20(I) was 60 units, 34 mg protein and GMA-EGDM 75-30(l) was 36 units, 21 mg protein/g polymer. The immobilized lipase matrices displayed enhanced pH, thermal, organic solvent and long-term storage stability. Both the immobilized enzyme matrices were tested firstly for the hydrolysis of triglycerides using tributyrin as substrate. After testing, both the matrices were reused for racemic resolution of ethyl-3-hydroxy-3-phenyl propanoate (fluoxetine intermediate, an antidepressant drug) and racemic chiral auxiliary, acetyl-1-phenyl ethanol (intermediate of many chiral drugs) for 15 cycles. These immobilized lipase matrices have shown very high stability on recycling, high-enantioselectivity, high conversion and faster recovery of product compare to free enzyme, therefore these matrices may find use in kinetic resolution process developments. (C) 2007 Elsevier Ltd. All rights reserved.</p>10a1-phenyl ethanol and enantioselectivity10achiral resolution10aenantiomeric excess (ee)10aethyl-3-hydroxy-3-phenyl propanoate10aImmobilization10aLipase1 aBhushan, Indu1 aParshad, Rajinder1 aQazi, Gulam, Nabi1 aIngavle, Ganesh, C.1 aRajan, C., R.1 aPonrathnam, Surendera1 aGupta, Vijay, Kumar  uhttps://library.ncl.res.in/content/lipase-enzyme-immobilization-synthetic-beaded-macroporous-copolymers-kinetic-resolution-0