4.7 Article

Shielding effects of Fe3+-tannic acid nanocoatings for immobilized enzyme on magnetic Fe3O4@silica core shell nanosphere

Journal

CHEMICAL ENGINEERING JOURNAL
Volume 343, Issue -, Pages 629-637

Publisher

ELSEVIER SCIENCE SA
DOI: 10.1016/j.cej.2018.03.002

Keywords

Supramolecular metal-phenolic nanocoating; Magnetic Fe3O4/silica core-shell nanospheres; Enzyme shielding strategy; Nanobiocatalysts

Funding

  1. National Natural Science Foundation of China [21676069]
  2. Foundation of Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education
  3. Tianjin Key Lab of Industrial Microbiology (Tianjin University of Science Technology) [2016IM001]
  4. Hundreds of outstanding innovative talents in Hebei province (III) [SLRC2017036]

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Enzyme immobilization on solid supports is a valuable approach to address enzyme stability and reuse for continuous operations. However, the enzymes immobilized on the external surface of solid supports may not be protected by carriers and suffer inactivation caused by denaturing stresses and hazard external environment. Herein, we describe for the first time a enzyme-shielding strategy to prepare hybrid organic/inorganic nano-biocatalysts; it exploits the self-assembly of supramolecular metal-organic coordination complex (tannic acid (TA) and Fe3+) at the surface of immobilized catalase on Fe3O4/silica core-shell nanospheres to grow a protective nanocoating (Fe3+-TA nanocoating). The nanocoatings around the immobilized catalase (Fe3+-TA@Fe3O4/SiO2-catalase) provide a shield effect to protect from biological, thermal and chemical degradation for enzyme. As a result, the stability of immobilized catalase against proteolytic agent, denaturants and heat were improved remarkably compared to the immobilized catalase without a protective nanocoating and free catalase. More importantly, the recycling of the immobilized catalase was improved remarkably. The Fe3+-TA@Fe3O4/SiO2-catalase still retained 55% of their original activity after 9 cycles, whereas the immobilized catalase without a protective nanocoating only retained 20% of original activity. These results demonstrated that the novel enzyme-shielding strategy is an efficient method to obtain stable and recycled biocatalyst with yolk-shell structure.

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