@article { ISI:000334421100007,
	title = {Protein-coated polymer as a matrix for enzyme immobilization: immobilization of trypsin on bovine serum albumin-coated allyl glycidyl ether-ethylene glycol dimethacrylate copolymer},
	journal = {Biotechnology Progress},
	volume = {30},
	number = {2},
	year = {2014},
	month = {MAR},
	pages = {317-323},
	publisher = {WILEY-BLACKWELL},
	address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
	abstract = {<p>Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25\% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16\% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel matrix with naturally existing functional groups such as thiol, amino, and carboxylic acid that are available for covalent immobilization of functional enzymes. Employing appropriate strategies, trypsin as a model protein was covalently bound to BSA-coated matrix both independently, and in a stepwise manner on the same matrix, with less than 5\% loss of enzyme activity during immobilization. Glutaraldehyde crosslinking after immobilization provide stable enzyme preparation with activity of 510 units/g recycled up to six times without loss of enzyme activity. AFM studies reveal that the polymer surface has protein peaks and valleys rather than a uniform monolayer distribution of the protein and the immobilized enzyme preparation can best be described as polymer supported cross-linked enzyme aggregates (CLEAs). (c) 2014 American Institute of Chemical Engineers Biotechnol. Prog., 30:317-323, 2014</p>},
	keywords = {allyl glycidyl ether, Bovine serum albumin, ethylene glycol dimethacrylate, Immobilization, Trypsin},
	issn = {8756-7938},
	doi = {10.1002/btpr.1871},
	author = {Jasti, Lakshmi Swarnalatha and Dola, Sandhya Rani and Kumaraguru, Thenkrishnan and Bajja, Sreedhar and Fadnavis, Nitin W. and Addepally, Uma and Rajdeo, Kishor and Ponrathnam, Surendra and Deokar, Sarika Babasaheb}
}
@article { ISI:000380625200002,
	title = {Immobilization of pectinase on reusable polymer support for clarification of apple juice},
	journal = {Food and Bioproducts Processing},
	volume = {99},
	year = {2016},
	month = {JUL},
	pages = {12-19},
	publisher = {INST CHEMICAL ENGINEERS},
	address = {165-189 RAILWAY TERRACE, DAVIS BLDG, RUGBY CV21 3HQ, ENGLAND},
	abstract = {<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>},
	keywords = {Apple juice, Dextran aldehyde, Immobilization, Pectinase, Polyethyleneimine, Polymer},
	issn = {0960-3085},
	doi = {10.1016/j.fbp.2016.03.004},
	author = {Rajdeo, Kishor and Harini, Tirunagari and Lavanya, Kuna and Fadnavis, Nitin W.}
}
