Adikane, H. V. and Thakar, D. M. (2010) Studies of Penicillin G Acylase Immobilization Using Highly Porous Cellulose-Based Polymeric Membrane. Appl Biochem Biotechnol, 160. pp. 1130-1145.

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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 UApp 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 UApp 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 Km value (47.4 mM) as well as similar optimum pH (7.2) and temperature (40°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.

Item Type: Article
Subjects: Biological Sciences
Depositing User: Dr. H.V. Adikane
Date Deposited: 21 Feb 2012 05:33
Last Modified: 21 Feb 2012 05:33

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