01663nas a2200253   4500008004100000022001400041245014500055210006900200260007300269300001200342490000700354520072000361653001701081653002001098653001101118653001701129653001701146100002501163700002201188700002501210700002101235700002601256856012701282       2008                        eng d  a1369-703X00aProduction and single step purification of cyclodextrin glycosyltransferase from alkalophilic bacillus firmus by ion exchange chromatography0 aProduction and single step purification of cyclodextrin glycosyl  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAY  a510-5150 v393 a<p>Production and purification of starch digesting cyclodextrin glycosyl transferase (CGTase) from alkalophilic Bacillus firmus was investigated. Fermentation was carried out in 141 bioreactor at 28 degrees C using a medium containing dextrin, yeast extract, peptone, (NH4)H2PO4 and MgSO4.7H(2)O. The extracellular enzyme was concentrated by tangential flow ultrafiltration. The concentrated enzyme was chromatographed using DEAE-sepharose and phenyl sepharose. DEAE-sepharose could be used to purify CGTase in a single step with 23.1 fold purification and 80.6% recovery. The enzyme obtained had homogeneity and the molecular weight was 76 kDa confirmed by SDS-PAGE. (c) 2007 Elsevier B.V. All rights reserved.</p>10aalkalophilic10aBacillus firmus10aCGTase10acyclodextrin10aPurification1 aSavergave, Laman, S.1 aMule, Santosh, S.1 aJogdand, Vitthal, V.1 aNene, Sanjay, N.1 aGadre, Ramchandra, V.  uhttps://library.ncl.res.in/content/production-and-single-step-purification-cyclodextrin-glycosyltransferase-alkalophilic-001975nas 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