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A facile and efficient method of enzyme immobilization on silica particles via Michael acceptor film coatings: immobilized catalase in a plug flow reactor

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Abstract

A novel method was developed for facile immobilization of enzymes on silica surfaces. Herein, we describe a single-step strategy for generating of reactive double bonds capable of Michael addition on the surfaces of silica particles. This method was based on reactive thin film generation on the surfaces by heating of impregnated self-curable polymer, alpha-morpholine substituted poly(vinyl methyl ketone) p(VMK). The generated double bonds were demonstrated to be an efficient way for rapid incorporation of enzymes via Michael addition. Catalase was used as model enzyme in order to test the effect of immobilization methodology by the reactive film surface through Michael addition reaction. Finally, a plug flow type immobilized enzyme reactor was employed to estimate decomposition rate of hydrogen peroxide. The highly stable enzyme reactor could operate continuously for 120 h at 30 °C with only a loss of about 36 % of its initial activity.

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Authors and Affiliations

  1. Biochemical Processing and Biomaterial Research Laboratory, Gazi University, 06500, Ankara, Turkey

    Gulay Bayramoglu & M. Yakup Arica

  2. Department of Chemistry, Faculty of Sciences, Gazi University, 06500, Ankara, Turkey

    Gulay Bayramoglu & Aysenur Genc

  3. School of Medicine, Istanbul Kemerburgaz University, 34217, Istanbul, Turkey

    V. Cengiz Ozalp

  4. Department of Chemistry, Istanbul Technical University, Maslak, 34469, Istanbul, Turkey

    Ahmet Ince & Niyazi Bicak

Authors
  1. Gulay Bayramoglu
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  2. M. Yakup Arica
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  3. Aysenur Genc
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  4. V. Cengiz Ozalp
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  5. Ahmet Ince
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  6. Niyazi Bicak
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Correspondence to Gulay Bayramoglu.

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Bayramoglu, G., Arica, M.Y., Genc, A. et al. A facile and efficient method of enzyme immobilization on silica particles via Michael acceptor film coatings: immobilized catalase in a plug flow reactor. Bioprocess Biosyst Eng 39, 871–881 (2016). https://doi.org/10.1007/s00449-016-1566-0

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  • DOI: https://doi.org/10.1007/s00449-016-1566-0

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