01975nas a2200217   4500008004100000022001400041245013800055210006900193260007300262300001200335490000700347520111400354653002601468653002801494653001901522100002801541700002401569700001901593700002101612856012401633       2012                        eng d  a1381-514800aPoly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) copolymer beads as support for covalent immobilization of L-aminoacylase0 aPolyallyl glycidyl ethercoethylene glycol dimethacrylate copolym  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcOCT  a687-6940 v723 a<p>Porous epoxy-activated copolymer beads were synthesized as support for the covalent immobilization of Aspergillus melleus L-aminoacylase. Here, a series of copolymer bead were synthesized using either glycidyl methacrylate (GMA) or ally] glycidyl ether (AGE) as monomer units and ethylene glycol dimethacrylate (EGDM) as cross-linking agent. The effect of monomer used and the effect of amount of cross-linking agent on covalent immobilization of aminoacylase were studied. Furthermore, the effect of porogen on immobilization of aminoacylase was also evaluated. AGE-co-EGDM copolymer beads gave higher binding of aminoacylase than GMA-co-EGDM copolymer beads. AGE-co-EGDM copolymer beads synthesized with lauryl alcohol as porogen and having 150% cross-linked density (i.e. AGE-(L)-150) gave maximum enzyme binding. Under optimum conditions, AGE-(L)-150 copolymer beads gave about 130 U/g of aminoacylase activity which corresponds to 72.24% of activity yield. Immobilized aminoacylase showed a broader pH, higher temperature and extended storage stability. (C) 2012 Elsevier Ltd. All rights reserved.</p>10aEnzyme immobilization10aEpoxy-activated support10aL-Aminoacylase1 aVaidya, Bhalchandra, K.1 aIngavle, Ganesh, C.1 aPonrathnam, S.1 aNene, Sanjay, N.  uhttps://library.ncl.res.in/content/polyallyl-glycidyl-ether-co-ethylene-glycol-dimethacrylate-copolymer-beads-support-002089nas a2200241   4500008004100000022001400041245011000055210006900165260007300234300001200307490000700319520116600326653002201492653003501514653001901549653002201568653002601590100002801616700002101644700002901665700002101694856013201715       2012                        eng d  a1381-117700aPreparation of cross-linked enzyme aggregates of L-aminoacylase via co-aggregation with polyethyleneimine0 aPreparation of crosslinked enzyme aggregates of Laminoacylase vi  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a184-1910 v743 a<p>L-Aminoacylase from Aspergillus melleus was co-aggregated with polyethyleneimine and subsequently cross-linked with glutaraldehyde to obtain aminoacylase-polyethyleneimine cross-linked enzyme aggregates (termed as AP-CLEA). Under the optimum conditions, AP-CLEA expressed 74.9% activity recovery and 81.2% aggregation yield. The said method of co-aggregation and cross-linking significantly improved the catalytic stability of L-aminoacylase with respect to temperature and storage. AP-CLEA were employed for enantioselective synthesis of three unnatural amino acids (namely: phenylglycine, homophenylalanine and 2-naphthylalanine) via chiral resolution of their ester-. amide- and N-acetyl derivatives. The enantioselectivity of AP-CLEA was the highest for hydrolysis of amino acid amides; was moderate for hydrolysis of N-acetyl amino acids and was the least for hydrolysis of amino acid esters. Furthermore, AP-CLEA were found to retain more than 92% of the initial activity after five consecutive batches of (RS)-homophenylalanine hydrolysis suggesting an adequate operational stability of the biocatalyst. (C) 2011 Elsevier B.V. All rights reserved.</p>10achiral resolution10aCross-linked enzyme aggregates10aL-Aminoacylase10aPolyethyleneimine10aUnnatural amino acids1 aVaidya, Bhalchandra, K.1 aKuwar, Suyog, S.1 aGolegaonkar, Sandeep, B.1 aNene, Sanjay, N.  uhttps://library.ncl.res.in/content/preparation-cross-linked-enzyme-aggregates-l-aminoacylase-co-aggregation-polyethyleneimine-0