02109nas a2200277   4500008004100000022001400041245011100055210006900166260008700235300001200322490000700334520109400341653002701435653002301462653001901485653002301504653002301527653002001550100001801570700002201588700002401610700003001634700002101664700002501685856012101710       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<p>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%).</p>10aArthrobacter sp lipase10aEnantioselectivity10aImmobilization10aKinetic resolution10aN-vinylpyrrolidone10asoluble polymer1 aChaubey, Asha1 aParshad, Rajinder1 aTaneja, Subhash, C.1 aDeokar, Sarika, Babasaheb1 aRaman, Rajan, C.1 aPonrathnam, Surendra  uhttps://library.ncl.res.in/content/immobilization-enantioselective-lipase-soluble-supports-kinetic-resolution-drug-001977nas a2200265   4500008004100000022001400041245021300055210006900268260007900337300001000416490001000426520089900436653002301335653002501358653002001383653001901403653001801422100003101440700002401471700002401495700001901519700001901538700002501557856012901582       2014                        eng d  a0141-022900aCo-immobilized glucose oxidase and beta-galactosidase on bovine serum albumin coated allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer as a biosensor for lactose determination in milk0 aCoimmobilized glucose oxidase and betagalactosidase on bovine se  a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcOCT  a67-730 v64-653 a<p>Bovine serum albumin (BSA) was adsorbed on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) at pH 8.0 (16% w/w). The amino, thiol and carboxylic acid functional groups available on protein coated surface were utilized for covalent immobilization of glucose oxidase and beta-galactosidase, both independently, and in a step-wise manner on the same matrix, with no more than 10% loss of enzyme activity during immobilization. Glutaraldehyde cross-linking after immobilization provided stable enzyme preparations. The pH-optima of the immobilized enzymes were similar to those for free enzyme but their thermal stability was vastly improved. The co-immobilized enzyme support was used as a biosensor for determination of lactose in milk with excellent reproducibility and reusability. (C) 2014 Elsevier Inc. All rights reserved.</p>10abeta-Galactosidase10aBovine serum albumin10aGlucose oxidase10aImmobilization10aLactose assay1 aJasti, Lakshmi, Swarnalath1 aDola, Sandhya, Rani1 aFadnavis, Nitin, W.1 aAddepally, Uma1 aDaniels, Siona1 aPonrathnam, Surendra  uhttps://library.ncl.res.in/content/co-immobilized-glucose-oxidase-and-beta-galactosidase-bovine-serum-albumin-coated-allyl-002358nas a2200301   4500008004100000022001400041245018500055210006900240260006700309300001200376490000700388520119500395653002501590653002501615653003501640653001901675653001201694100003101706700002401737700002901761700002001790700002401810700001901834700001901853700002501872700003001897856012901927       2014                        eng d  a8756-793800aProtein-coated polymer as a matrix for enzyme immobilization: immobilization of trypsin on bovine serum albumin-coated allyl glycidyl ether-ethylene glycol dimethacrylate copolymer0 aProteincoated polymer as a matrix for enzyme immobilization immo  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcMAR  a317-3230 v303 a<p>Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel matrix with naturally existing functional groups such as thiol, amino, and carboxylic acid that are available for covalent immobilization of functional enzymes. Employing appropriate strategies, trypsin as a model protein was covalently bound to BSA-coated matrix both independently, and in a stepwise manner on the same matrix, with less than 5% loss of enzyme activity during immobilization. Glutaraldehyde crosslinking after immobilization provide stable enzyme preparation with activity of 510 units/g recycled up to six times without loss of enzyme activity. AFM studies reveal that the polymer surface has protein peaks and valleys rather than a uniform monolayer distribution of the protein and the immobilized enzyme preparation can best be described as polymer supported cross-linked enzyme aggregates (CLEAs). (c) 2014 American Institute of Chemical Engineers Biotechnol. Prog., 30:317-323, 2014</p>10aallyl glycidyl ether10aBovine serum albumin10aethylene glycol dimethacrylate10aImmobilization10aTrypsin1 aJasti, Lakshmi, Swarnalath1 aDola, Sandhya, Rani1 aKumaraguru, Thenkrishnan1 aBajja, Sreedhar1 aFadnavis, Nitin, W.1 aAddepally, Uma1 aRajdeo, Kishor1 aPonrathnam, Surendra1 aDeokar, Sarika, Babasaheb  uhttps://library.ncl.res.in/content/protein-coated-polymer-matrix-enzyme-immobilization-immobilization-trypsin-bovine-serum-0