@article { ISI:000342257000011,
	title = {Co-immobilized glucose oxidase and beta-galactosidase on bovine serum albumin coated allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer as a biosensor for lactose determination in milk},
	journal = {Enzyme and Microbial Technology},
	volume = {64-65},
	year = {2014},
	month = {OCT},
	pages = {67-73},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Bovine serum albumin (BSA) was adsorbed on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25\% crosslink density (AGE-25) at pH 8.0 (16\% w/w). The amino, thiol and carboxylic acid functional groups available on protein coated surface were utilized for covalent immobilization of glucose oxidase and beta-galactosidase, both independently, and in a step-wise manner on the same matrix, with no more than 10\% loss of enzyme activity during immobilization. Glutaraldehyde cross-linking after immobilization provided stable enzyme preparations. The pH-optima of the immobilized enzymes were similar to those for free enzyme but their thermal stability was vastly improved. The co-immobilized enzyme support was used as a biosensor for determination of lactose in milk with excellent reproducibility and reusability. (C) 2014 Elsevier Inc. All rights reserved.</p>},
	keywords = {beta-Galactosidase, Bovine serum albumin, Glucose oxidase, Immobilization, Lactose assay},
	issn = {0141-0229},
	doi = {10.1016/j.enzmictec.2014.07.005},
	author = {Jasti, Lakshmi Swarnalatha and Dola, Sandhya Rani and Fadnavis, Nitin W. and Addepally, Uma and Daniels, Siona and Ponrathnam, Surendra}
}
@article { ISI:000335706100026,
	title = {Comparison of polymer induced and solvent induced trypsin denaturation: the role of hydrophobicity},
	journal = {Colloids and Surfaces B-Biointerfaces},
	volume = {116},
	year = {2014},
	month = {APR},
	pages = {201-205},
	publisher = {ELSEVIER SCIENCE BV},
	type = {Article},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Trypsin adsorption from aqueous buffer by various copolymers of allyl glycidyl ether-ethylene glycol dimethacrylate (AGE-EGDM) copolymer with varying crosslink density increases with increasing crosslink density and the effect slowly wears off after reaching a plateau at 50\% crosslink density. The copolymer with 25\% crosslink density was reacted with different amines with alkyl/aryl side chains to obtain a series of copolymers with 1,2-amino alcohol functional groups and varying hydrophobicity. Trypsin binding capacity again increases with hydrophobicity of the reacting amine and a good correlation between logP(octanol) of the amine and protein binding is observed. The bound trypsin is denatured to the extent of 90\% in spite of the presence of hydrophilic hydroxyl and amino groups. The behavior was comparable to that in mixtures of aqueous buffer and water-miscible organic co-solvents where the solvent concentration required to deactivate 50\% of the enzyme (C-50) is dependent on logP(octanol) of the co-solvent. (C) 2014 Elsevier B.V. All rights reserved.</p>},
	keywords = {Adsorption, Denaturation, Hydrophobicity, Polymer, Trypsin},
	issn = {0927-7765},
	doi = {10.1016/j.colsurfb.2014.01.002},
	author = {Jasti, Lakshmi Swarnalatha and Fadnavis, Nitin W. and Addepally, Uma and Daniels, Siona and Deokar, Sarika Babasaheb and Ponrathnam, Surendra}
}
