@article { ISI:000309096400004,
	title = {Poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) copolymer beads as support for covalent immobilization of L-aminoacylase},
	journal = {Reactive \& Functional Polymers},
	volume = {72},
	number = {10},
	year = {2012},
	month = {OCT},
	pages = {687-694},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<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>},
	keywords = {Enzyme immobilization, Epoxy-activated support, L-Aminoacylase},
	issn = {1381-5148},
	doi = {10.1016/j.reactfunctpolym.2012.06.012},
	author = {Vaidya, Bhalchandra K. and Ingavle, Ganesh C. and Ponrathnam, S. and Nene, Sanjay N.}
}
@article { ISI:000300036000006,
	title = {Preparation of cross-linked enzyme aggregates of L-aminoacylase via co-aggregation with polyethyleneimine},
	journal = {Journal of Molecular Catalysis B-Enzymatic},
	volume = {74},
	number = {3-4},
	year = {2012},
	month = {FEB},
	pages = {184-191},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<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>},
	keywords = {chiral resolution, Cross-linked enzyme aggregates, L-Aminoacylase, Polyethyleneimine, Unnatural amino acids},
	issn = {1381-1177},
	doi = {10.1016/j.molcatb.2011.10.003},
	author = {Vaidya, Bhalchandra K. and Kuwar, Suyog S. and Golegaonkar, Sandeep B. and Nene, Sanjay N.}
}
