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Noncovalent immobilization of MnP from on carbon nanotubes |
Jiaxi LI , Xianghua WEN , |
SKLESPC, Department
of Environmental Science and Engineering, Tsinghua University, Beijing
100084, China; |
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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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Keywords
manganese peroxidases (MnP)
Phanerochaete chrysosporium
carbon nanotubes
immobilization
catalytic activity
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Issue Date: 05 September 2009
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