Characteristics of Penicillin G Acylase Immobilized onto Iron Oxide Nanoparticles
Journal Title: Biotechnology Journal International - Year 2013, Vol 3, Issue 3
Abstract
Penicillin G acylase was immobilized onto iron oxide nanoparticles coated with polyethyleneimine and then cross linked with glutaraldehyde solution. The FTIR spectrum of immobilized enzyme showed peak at 1648cm-1 which can be attributed to the C=N bonds of Schiff’s base linkage formed between glutaraldehyde and amino group of penicillin G acylase. By considering the FTIR spectrum of nano particle coated with polyethyleneimine, adsorption of penicillin G acylase has taken place and then glutaraldehyde cross linked enzyme onto activated support. Catalytic properties of nano penicillin G acylase were improved upon immobilization as compared to its free counterpart. The optimal pH and temperature were determined to be 7.0, 10.0, 50 and 75ºC for free and immobilized penicillin G acylase, respectively. Thermal stabilities of both nano and free penicillin G acylase were studied .The Km value of immobilized nanozyme was calculated from Lineweaver Burck plot to be 0.23 μM while that of free penicillin G acylase was 0.28μM. In this way nano penicillin G acylase with improved catalytic properties was developed as compared to its soluble counterpart.
Authors and Affiliations
Norouzian Dariush, Momen Seyed Bahman, Atyabi Seyed Mohammad, Azim Akbarzadeh, Salimi Mona, Sedigeh Hatami Gigloo, Farhangi Ali
Keywords
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- EP ID EP237115
- DOI 10.9734/BBJ/2013/2987
- Views 159
- Downloads 0
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