Chinese Journal of Catalysis ›› 2016, Vol. 37 ›› Issue (4): 584-595.DOI: 10.1016/S1872-2067(15)61045-2

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A magnetic biocatalyst based on mussel-inspired polydopamine and its acylation of dihydromyricetin

Xiao Denga,c, Shilin Caob,c, Ning Lic, Hong Wuc, Thomas J. Smithd, Minhua Zonga,b, Wenyong Loua,c   

  1. a State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, Guangdong, China;
    b School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, Guangdong, China;
    c Laboratory of Applied Biocatalysis, School of Food Science and Technology, South China University of Technology, Guangzhou 510640, Guangdong, China;
    d Biomolecular Sciences Research Centre, Sheffield Hallam University, Sheffield, S1 1WB, UK
  • Received:2015-11-01 Revised:2016-01-04 Online:2016-03-30 Published:2016-03-30
  • Contact: Thomas J. Smith, Wenyong Lou
  • Supported by:

    This work was supported by the National Natural Science Foundation of China(21336002, 21222606, 21376096), the Key Program of Guangdong Natural Science Foundation(S2013020013049), the Fundamental Research Funds for the Chinese Universities(2015PT002, 2015ZP009), and the Program of State Key Laboratory of Pulp and Paper Engineering(2015C04).


A support made of mussel-inspired polydopamine-coated magnetic iron oxide nanoparticles (PD-MNPs) was prepared and characterized. The widely used Aspergillus niger lipase (ANL) was immobilized on the PD-MNPs (ANL@PD-MNPs) with a protein loading of 138 mg/g and an activity recovery of 83.6% under optimized conditions. For the immobilization, the pH and immobilization time were investigated. The pH and thermal and storage stability of the ANL@PD-MNPs significantly surpassed those of free ANL. The ANL@PD-MNPs had better solvent tolerance than free ANL. The secondary structure of free ANL and ANL@PD-MNPs was analyzed by infrared spectroscopy. A kinetic study demonstrated that the ANL@PD-MNPs had enhanced enzyme-substrate affinity and high catalytic efficiency. The ANL@PD-MNPs was applied as a biocatalyst for the regioselective acylation of dihydromyricetin (DMY) in DMSO and gave a conversion of 79.3%, which was higher than that of previous reports. The ANL@PD-MNPs retained over 55% of its initial activity after 10 cycles of reuse. The ANL@PD-MNPs were readily separated from the reaction system by a magnet. The PD-MNPs is an excellent support for ANL and the resulting ANL@PD-MNPs displayed good potential for the efficient synthesis of dihydromyricetin-3-acetate by enzymatic regioselective acylation.

Key words: Magnetic iron oxide, Nanoparticle, Polydopamine, Aspergillus niger lipase, Dihydromyricetin, Acylation