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- W2313648713 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 Schiffs 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 75∫C 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 �oM while that of free penicillin G acylase was 0.28�oM. In this way nano penicillin G acylase with improved catalytic properties was developed as compared to its soluble counterpart." @default.
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- W2313648713 date "2013-01-10" @default.
- W2313648713 modified "2023-10-16" @default.
- W2313648713 title "Characteristics of Penicillin G Acylase Immobilized onto Iron Oxide Nanoparticles" @default.
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- W2313648713 doi "https://doi.org/10.9734/bbj/2013/2987" @default.
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