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

    New search for: Li, Jiaxi
    New search for: Wen, Xianghua

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

    New search for: Li, Jiaxi
    New search for: Wen, Xianghua

    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.

    Access

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

    New search for: Li, Jiaxi
    New search for: Wen, Xianghua

    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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    Title:

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

    Contributors:

    Li, Jiaxi (author) / Wen, Xianghua (author)

    Published in:

    Frontiers of Environmental Science & Engineering in China ; 3 ; 294-299

    Publication date:

    2009-07-29

    Size:

    6 pages

    ISSN:

    1673-7520 , 1673-7415

    DOI:

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

    Type of media:

    Article (Journal)

    Type of material:

    Electronic Resource

    Language:

    English

    Keywords:

    manganese peroxidases (MnP) , Phanerochaete chrysosporium , carbon nanotubes , immobilization , catalytic activity Environment , Environment, general

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