02089nas 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-002180nas a2200253   4500008004100000022001400041245009300055210006900148260009500217300001000312490000700322520129400329653001601623653002101639653001901660653001401679653002201693653001201715100001901727700002301746700001801769700002401787856011501811       2016                        eng d  a0960-308500aImmobilization of pectinase on reusable polymer support for clarification of apple juice0 aImmobilization of pectinase on reusable polymer support for clar  a165-189 RAILWAY TERRACE, DAVIS BLDG, RUGBY CV21 3HQ, ENGLANDbINST CHEMICAL ENGINEERScJUL  a12-190 v993 a<p>Pectinase (E.C.3.2.1.15) was successfully immobilized on recyclable polymer matrix. The immobilization matrix was prepared by reaction of polyethyleneimine (mol. wt. 70,000) with epoxy-activated acrylate copolymer DILBEAD-VWR. The enzyme pectinase was first adsorbed on the polymer at pH 7.0 via ion exchange and then stabilized by crosslinking with dextran aldehyde. While the free enzyme shows a pH-optimum of 5.0, the immobilized enzyme exhibited high level of activity in a broad pH range of pH 3.0-7.0. Although the thermal stability of free and immobilized enzymes was similar, at room temperature, the immobilized enzyme could be recycled more than 10 times with loss of less than 5% of its activity during clarification of apple juice. On the eventual loss of enzyme activity, the immobilized enzyme and dextran aldehyde can be easily removed from the polymer by a simple treatment with 1N HCl and the polymer can be reused for immobilization of a fresh batch of enzyme. This support also can be reused several times, making the process economically attractive. The properties of apple juice treated with immobilized enzyme were similar to those of that treated with free pectinase. (C) 2016 Institution of Chemical Engineers. Published by Elsevier B.V. All rights reserved.</p>10aApple juice10aDextran aldehyde10aImmobilization10aPectinase10aPolyethyleneimine10aPolymer1 aRajdeo, Kishor1 aHarini, Tirunagari1 aLavanya, Kuna1 aFadnavis, Nitin, W.  uhttps://library.ncl.res.in/content/immobilization-pectinase-reusable-polymer-support-clarification-apple-juice01944nas a2200229   4500008004100000022001400041245013300055210006900188260000800257300000800265490000700273520115000280653001401430653001701444653002401461653001701485653002201502100002401524700001901548700002301567856012401590       2021                        eng d  a1022-976000aFabrication of bacterial nanocellulose/polyethyleneimine (PEI-BC) based cationic adsorbent for efficient removal of anionic dyes0 aFabrication of bacterial nanocellulosepolyethyleneimine PEIBC ba  cSEP  a3540 v283 aA bacterial cellulose (BC) based adsorbent was prepared by using polyethyleneimine (PEI) using epichlorohydrin as a cross-linker. The physicochemical characterization of the of the developed adsorbent was carried out using FTIR, BET analysis and SEM, respectively. The dye removal efficiency of the adsorbent was assessed towards two anionic model dyes viz. congo red (CR) and reactive red 120(RR). The kinetic data for the removal of both the anionic dyes were fitted better using pseudo-second-order model. Langmuir model describes well the process of adsorption with predicted maximum adsorption capacity (q(max)) 515.46 and 300.3 mg L-1 for CR (at pH 6.0) and RR (at pH 3.0) respectively. The adsorption-desorption study showed that PEI-BC adsorbent is effective with more than 90% dye removal efficiency even after four cycles. Furthermore, the bactericidal activity of the adsorbent was analysed using Escherichia coli and Staphylococcus aureus and adsorbent showed good inhibition against both test organisms. The study reveals that PEI-BC adsorbent can be a good candidate for water remediation purpose bearing multifunctional behaviour.10aadsorbent10aAnionic dyes10aBacterial cellulose10aBactericidal10aPolyethyleneimine1 aThorat, Meghana, N.1 aJagtap, Ashish1 aDastager, Syed, G.  uhttps://library.ncl.res.in/content/fabrication-bacterial-nanocellulosepolyethyleneimine-pei-bc-based-cationic-adsorbent