Chinese Journal of Catalysis ›› 2013, Vol. 34 ›› Issue (4): 723-733.DOI: 10.1016/S1872-2067(12)60564-6

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Catalytic performance and stability of C-C bond hydrolase BphD immobilized onto single-wall carbon nanotubes

SHEN E, QU Yuanyuan, ZHOU Hao, KONG Chunlei, MA Qiao, ZHANG Xuwang, ZHOU Jiti   

  1. Key Laboratory of Industrial Ecology and Environmental Engineering, Ministry of Education, School of Environmental Science and Technology, Dalian University of Technology, Dalian 116024, Liaoning, China
  • Received:2012-12-21 Revised:2013-02-27 Online:2013-04-23 Published:2013-04-24
  • Supported by:

    This work was supported by the National Natural Science Foundation of China (51078054, 21176040).

Abstract:

Single-wall carbon nanotubes (SWCNTs) possess unique mechanical properties and extraordinary thermal conductivity, and were used as the matrix for immobilized biocatalysts. The C-C bond hydrolase BphD was immobilized on SWCNTs by physical adsorption and covalent bonding. The relative activity, stability, and reusability of the immobilized enzyme were investigated. BphD immobilized by physical adsorption retained 52.5% of the activity of free BphD, and BphD thermal stability and denaturant resistance were also improved. Covalently bound BphD exhibited the activity nearly the same as that of free BphD (99.7% of initial activity), but its stability showed no significant improvement over that of free BphD.

Key words: C-C bond hydrolase, Single-wall carbon nanotube, Immobilization, Molecular simulation, Physical adsorption, Covalent bonding