@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.}
}
@article { ISI:000325608800002,
	title = {Proteome wide reduction in AGE modification in streptozotocin induced diabetic mice by hydralazine mediated transglycation},
	journal = {Scientific Reports},
	volume = {3},
	year = {2013},
	month = {OCT},
	pages = {2941},
	publisher = {NATURE PUBLISHING GROUP},
	address = {MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND},
	abstract = {<p>The non-enzymatic reaction between glucose and protein can be chemically reversed by transglycation. Here we report the transglycation activity of hydralazine using a newly developed MALDI-TOF-MS based assay. Hydralazine mediated transglycation of HbA1c, plasma proteins and kidney proteins was demonstrated in streptozotocin (STZ) induced diabetic mice, as evidenced by decrease in protein glycation, as well as presence of hydralazine-glucose conjugate in urine of diabetic mice treated with hydralazine. Hydralazine down regulated the expression of Receptor for Advanced Glycation End products (RAGE), NADPH oxidase (NOX), and super oxide dismutase (SOD). These findings will provide a new dimension for developing intervention strategies for the treatment of glycation associated diseases such as diabetes complications, atherosclerosis, and aging.</p>},
	issn = {2045-2322},
	doi = {10.1038/srep02941},
	author = {Kesavan, Suresh K. and Bhat, Shweta and Golegaonkar, Sandeep B. and Jagadeeshaprasad, Mashanipalya G. and Deshmukh, Arati B. and Patil, Harshal S. and Bhosale, Santosh D. and Shaikh, Mahemud L. and Thulasiram, Hirekodathakallu V. and Boppana, Ramanamurthy and Kulkarni, Mahesh J.}
}
