@article { ISI:000274398400016,
	title = {Studies of penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane},
	journal = {Applied Biochemistry and Biotechnology},
	volume = {160},
	number = {4},
	year = {2010},
	month = {FEB},
	pages = {1130-1145},
	publisher = {HUMANA PRESS INC},
	address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA},
	abstract = {<p>The different ionic molecules/compounds were used as a ligand for the immobilization of penicillin G acylase on the highly porous cellulose-based polymeric membrane having buffer flux 1,746 LMH (L m(-2) h(-1)) at 0.5 bar pressure. The immobilized enzyme activity around 250 U-App was obtained with the ligand such as proline, tryptophan, casein acid hydrolysate, and brilliant green. Comparatively, proline showed less IMY\% (percentage immobilization yield-58) but higher RTA\% (percentage of activity retention-71) and specific activity (145 U-App g(-1)). However, the crosslinked preparation of brilliant green obtained using glutaraldehyde showed 82 +/- 2.7\% immobilized enzyme activity after the completion of successive five cycles. In comparison with the free enzyme, the enzyme immobilized on the brilliant green coupled membrane showed around 2.4-fold increase in K-m value (47.4 mM) as well as similar optimum pH (7.2) and temperature (40 degrees C). The immobilized enzyme retained almost 50\% activity after 107 days and 50 cycles of operation. Almost 50\% decrease in buffer flux after enzyme immobilization was observed. At the end of the 30 cycles, flux pattern shows around 38\% decrease in buffer flux however, after 16 cycles of operation flux moves closer towards the steady state.</p>},
	keywords = {Brilliant green, Immobilization, Penicillin G acylase, Polymeric membrane, Proline},
	issn = {0273-2289},
	doi = {10.1007/s12010-009-8686-9},
	author = {Adikane, H. V. and Thakar, D. M.}
}
