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Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes

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Abstract

Chloroperoxidase (CPO) from Caldariomyces fumago was optimally covalently immobilized on chitosan membranes pretreated with 0.8 M glutaraldehyde at pH 3.5 to give 3.18 mg CPO g−1 support. Using monochlorodimedone (MCD) as assay substrate, the immobilized-CPO retained 40% activity at 50°C after 40 min whereas free CPO retained only 0.02%. The residual activity for immobilized-CPO was 99 and 58% compared with 68 and 43% for free CPO in the presence of 1.5 M urea and 300 μM H2O2, respectively, after 20 h.

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Acknowledgements

This work is supported by the National Natural Science Foundation of China (20876094).

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Authors and Affiliations

  1. Key Laboratory of Macromolecular Science of Shaanxi Province, Shaanxi Normal University, Xi’an, Shaanxi, People’s Republic of China

    Yu-Cheng Jiang, Man-Cheng Hu, Shu-Ni Li & Quan-Guo Zhai

  2. School of Chemistry and Materials Science, Shaanxi Normal University, Chang’an South Road, 199, Xi’an, Shaanxi, 710062, People’s Republic of China

    Li-Hua Zhang, Chao-Hong Bai, Ying-Song Wang, Yu-Cheng Jiang, Man-Cheng Hu, Shu-Ni Li & Quan-Guo Zhai

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  1. Li-Hua Zhang
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  2. Chao-Hong Bai
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  3. Ying-Song Wang
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  4. Yu-Cheng Jiang
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  5. Man-Cheng Hu
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  6. Shu-Ni Li
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  7. Quan-Guo Zhai
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Correspondence to Yu-Cheng Jiang.

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Zhang, LH., Bai, CH., Wang, YS. et al. Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes. Biotechnol Lett 31, 1269–1272 (2009). https://doi.org/10.1007/s10529-009-0009-2

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  • DOI: https://doi.org/10.1007/s10529-009-0009-2

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