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Stability improvement of immobilized lactoperoxidase using polyaniline polymer |
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| Authors: | Fariba Jafary Soheila Kashanian Ziadin Samsam Sharieat Farzaneh Jafary Kobra Omidfar Maliheh Paknejad |
| Affiliation: | 1. Department of Biology, Faculty of Science, Razi University, Kermanshah, Iran 2. Faculty of Chemistry, Nanoscience and Nanotechnology Research Center (NNRC) and Sensor and Biosensor Research Center (SBRC), Razi University, P.O. Box 67149, Kermanshah, Iran 3. Department of Biology, University of Medical Sciences, Isfahan, Iran 4. Department of Biology, Faculty of Science, Alzahra University, Tehran, Iran 5. Endocrinology and Metabolism Research Center, Tehran University of Medical Sciences, Tehran, Iran 6. Department of Biochemistry, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran |
| Abstract: | Enzyme engineering via immobilization techniques is perfectly compatible against the other chemical or biological approximate to improve enzyme functions and stability. In this study lactoperoxidase was immobilized onto polyaniline polymer activated with glutaraldehyde as a bifunctional agent, to improve enzyme properties. Polyaniline polymer was used due its unique physical and chemical properties to immobilize lactoperoxidase (LPO). The optimum activity of immobilized LPO was observed at pH 6 and 55?°C, which has been increased about 10?°C for the immobilized enzyme. The immobilized enzyme maintained absolutely active for 60?days whereas the native enzyme lost 80?% of its initial activity within this period of time. Moreover, the immobilized enzyme can be reused for several times without loss of activity. The kinetic parameter studies showed slight differences between free and immobilized enzymes. The Km and Km.app were calculated to be 0.6 and 0.4; also Vmax and Vmax.app were 1.3 and 0.9 respectively. |
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