01977nas 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-002020nas a2200265   4500008004100000022001400041245010300055210006900158260007300227300001200300490000800312520108200320653001501402653001701417653001901434653001201453653001201465100003101477700002401508700001901532700001901551700003001570700002501600856012901625       2014                        eng d  a0927-776500aComparison of polymer induced and solvent induced trypsin denaturation: the role of hydrophobicity0 aComparison of polymer induced and solvent induced trypsin denatu  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAPR  a201-2050 v1163 a<p>Trypsin adsorption from aqueous buffer by various copolymers of allyl glycidyl ether-ethylene glycol dimethacrylate (AGE-EGDM) copolymer with varying crosslink density increases with increasing crosslink density and the effect slowly wears off after reaching a plateau at 50% crosslink density. The copolymer with 25% crosslink density was reacted with different amines with alkyl/aryl side chains to obtain a series of copolymers with 1,2-amino alcohol functional groups and varying hydrophobicity. Trypsin binding capacity again increases with hydrophobicity of the reacting amine and a good correlation between logP(octanol) of the amine and protein binding is observed. The bound trypsin is denatured to the extent of 90% in spite of the presence of hydrophilic hydroxyl and amino groups. The behavior was comparable to that in mixtures of aqueous buffer and water-miscible organic co-solvents where the solvent concentration required to deactivate 50% of the enzyme (C-50) is dependent on logP(octanol) of the co-solvent. (C) 2014 Elsevier B.V. All rights reserved.</p>10aAdsorption10aDenaturation10aHydrophobicity10aPolymer10aTrypsin1 aJasti, Lakshmi, Swarnalath1 aFadnavis, Nitin, W.1 aAddepally, Uma1 aDaniels, Siona1 aDeokar, Sarika, Babasaheb1 aPonrathnam, Surendra  uhttps://library.ncl.res.in/content/comparison-polymer-induced-and-solvent-induced-trypsin-denaturation-role-hydrophobicity-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