<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chaubey, Asha</style></author><author><style face="normal" font="default" size="100%">Parshad, Rajinder</style></author><author><style face="normal" font="default" size="100%">Taneja, Subhash C.</style></author><author><style face="normal" font="default" size="100%">Deokar, Sarika Babasaheb</style></author><author><style face="normal" font="default" size="100%">Raman, Rajan C.</style></author><author><style face="normal" font="default" size="100%">Ponrathnam, Surendra</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Immobilization of enantioselective lipase on soluble supports for kinetic resolution of drug intermediates</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Bioactive and Compatible Polymers</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Arthrobacter sp lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Enantioselectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetic resolution</style></keyword><keyword><style  face="normal" font="default" size="100%">N-vinylpyrrolidone</style></keyword><keyword><style  face="normal" font="default" size="100%">soluble polymer</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</style></number><publisher><style face="normal" font="default" size="100%">SAGE PUBLICATIONS LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">1 OLIVERS YARD, 55 CITY ROAD, LONDON EC1Y 1SP, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">499-509</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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%).&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.207
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jasti, Lakshmi Swarnalatha</style></author><author><style face="normal" font="default" size="100%">Dola, Sandhya Rani</style></author><author><style face="normal" font="default" size="100%">Fadnavis, Nitin W.</style></author><author><style face="normal" font="default" size="100%">Addepally, Uma</style></author><author><style face="normal" font="default" size="100%">Daniels, Siona</style></author><author><style face="normal" font="default" size="100%">Ponrathnam, Surendra</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Co-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 milk</style></title><secondary-title><style face="normal" font="default" size="100%">Enzyme and Microbial Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">beta-Galactosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Bovine serum albumin</style></keyword><keyword><style  face="normal" font="default" size="100%">Glucose oxidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword><keyword><style  face="normal" font="default" size="100%">Lactose assay</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE INC</style></publisher><pub-location><style face="normal" font="default" size="100%">360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA</style></pub-location><volume><style face="normal" font="default" size="100%">64-65</style></volume><pages><style face="normal" font="default" size="100%">67-73</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.624</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jasti, Lakshmi Swarnalatha</style></author><author><style face="normal" font="default" size="100%">Dola, Sandhya Rani</style></author><author><style face="normal" font="default" size="100%">Kumaraguru, Thenkrishnan</style></author><author><style face="normal" font="default" size="100%">Bajja, Sreedhar</style></author><author><style face="normal" font="default" size="100%">Fadnavis, Nitin W.</style></author><author><style face="normal" font="default" size="100%">Addepally, Uma</style></author><author><style face="normal" font="default" size="100%">Rajdeo, Kishor</style></author><author><style face="normal" font="default" size="100%">Ponrathnam, Surendra</style></author><author><style face="normal" font="default" size="100%">Deokar, Sarika Babasaheb</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein-coated polymer as a matrix for enzyme immobilization: immobilization of trypsin on bovine serum albumin-coated allyl glycidyl ether-ethylene glycol dimethacrylate copolymer</style></title><secondary-title><style face="normal" font="default" size="100%">Biotechnology Progress</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">allyl glycidyl ether</style></keyword><keyword><style  face="normal" font="default" size="100%">Bovine serum albumin</style></keyword><keyword><style  face="normal" font="default" size="100%">ethylene glycol dimethacrylate</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypsin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">WILEY-BLACKWELL</style></publisher><pub-location><style face="normal" font="default" size="100%">111 RIVER ST, HOBOKEN 07030-5774, NJ USA</style></pub-location><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">317-323</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.65</style></custom4></record></records></xml>