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

BAYRAMOĞLU G., Arica M. Y., Genc A., Ozalp V. C., Ince A., Bicak N.

BIOPROCESS AND BIOSYSTEMS ENGINEERING, cilt.39, sa.6, ss.871-881, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 39 Sayı: 6
  • Basım Tarihi: 2016
  • Doi Numarası: 10.1007/s00449-016-1566-0
  • Dergi Adı: BIOPROCESS AND BIOSYSTEMS ENGINEERING
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.871-881
  • Anahtar Kelimeler: Michael addition, Surface modification, Catalase, Immobilized enzymes, Enzyme bioreactors, COVALENT IMMOBILIZATION, SURFACE, OPTIMIZATION, STABILITY, COMPOSITE, POLYMERS, CHITOSAN, LIPASE, BEADS
  • Gazi Üniversitesi Adresli: Evet

Özet

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 degrees C with only a loss of about 36 % of its initial activity.