@conference {42804,
	title = {Poly(High Internal Phase Emulsion) of 2-EHA, 2-EHMA and EGDA with naturally occurring phenolic compounds", paper presented at international conference on ?polymers for advanced technology},
	booktitle = {Polymers for Advanced Technology},
	year = {2006},
	month = {DEC},
	address = {National Chemical Laboratory, Pune},
	author = {Ingavle, Ganesh C. and Shaikh, A. A. and Bhongale, Sunil Sitaram and Scaria, S. and Chavan, Nayaku and Qureshi, Mohammed and Ponrathnam, Surendra}
}
@article {42795,
	title = {Process for synthesis of beaded cross linked polymers, water-in-oil-in-water emulsions and post functionalisation},
	number = {2538/DEL},
	year = {2010},
	month = {JAN},
	author = {Dwivedi, Mayank and Rao, Locanindi Hari Sarvothama and Reddy, Krishna Mohan Srinivasulu and Dhanasekharan, Janakiraman and Rao, Bevara Madhusudana and Kumar, Sriperambudur Rajesh and Ponrathnam, Surendra and Chelanattukizhakkemadath, Raman Rajan and Tayal, Rajivkumar and Qureshi, Moham}
}
@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}
}
