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Noncovalent immobilization of manganese peroxidases from P. chrysosporium on carbon nanotubes

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Abstract

Manganese peroxidases (MnP) from Phanerochaete chrysosporium were adsorbed onto multi-walled carbon nanotubes (MWNT). Four different loadings of MnP on MWNTs were investigated, and the maximum enzyme loading of 47.5 μg/mg of MWNTs was obtained in 12 h. The adsorbed MnP showed a catalytic activity of up to 0.1 U/mg of the weight of the system of MnP/MWNTs, with 23% of its original activity retained. The AFM image of the adsorbed enzymes indicated that a layer of MnP covered the surface of the MWNTs and retained its original three-dimensional shape. Amino-based nonspecific interactions may play the dominant role in the adsorption of MnP on MWNTs.

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Authors and Affiliations

  1. SKLESPC, Department of Environmental Science and Engineering, Tsinghua University, Beijing, 100084, China

    Jiaxi Li & Xianghua Wen

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  1. Jiaxi Li
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  2. Xianghua Wen
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Correspondence to Xianghua Wen.

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Li, J., Wen, X. Noncovalent immobilization of manganese peroxidases from P. chrysosporium on carbon nanotubes. Front. Environ. Sci. Eng. China 3, 294–299 (2009). https://doi.org/10.1007/s11783-009-0041-4

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  • DOI: https://doi.org/10.1007/s11783-009-0041-4

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