Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

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

  • 549 Accesses

  • 11 Citations

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.

This is a preview of subscription content, log in to check access.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

References

  1. 1.

    Brinkman RP, Kratzer M, Schmidt H (1999) Simulation of plasma processes for microelectronic fabrication. Pure Appl Chem 71:1863–1869

  2. 2.

    Yi S, Kim J-K, Yue CY, Hsieh J-H (2000) Bonding strengths at plastic encapsulant gold plated copper-lead frame interface. Microelectron Reliab 40:1207–1214

  3. 3.

    Suzuki Y (2003) Ion beam modification of polymers for the application of medical devices. Nucl Instrum Meth B 206:501–506

  4. 4.

    Liston EM, Martinu L, Wertheimer MR (1993) Plasma surface modification of polymers for improved adhesion: a critical review. Adhes Sci Techol 7:1091–1127

  5. 5.

    Grzegorzewski F, Rohn S, Quade A, Schroder K, Ehlbeck J, Schluter O, Kroh LW (2010) Reaction chemistry of 1,4-benzopyrone derivates in non-equilibrium low-temperature plasmas. Plasma Process Polym 7:466–473

  6. 6.

    Bicak N (2014) A facile method for generating Michael acceptor thin films via amine substituted poly(vinyl methyl ketone). Pure Appl Chem 86:1829–1838

  7. 7.

    Bayramoglu G, Arica MY (2010) Reversible immobilization of catalase on Fe(III) chelated poly(itaconic acid) grafted chitosan membranes. J Mol Catal B 62:297–304

  8. 8.

    Todero LM, Bassi JJ, Lage FAP, Corradini MCC, Barboza JCS, Hirata DB, Mendes AA (2015) Enzymatic synthesis of isoamyl butyrate catalyzed by immobilized lipase on poly-methacrylate particles: optimization, reusability and mass transfer studies. Bioprocess Biosyst Eng 38:1601–1613. doi:10.1007/s00449-015-1402-y

  9. 9.

    Bayramoglu G, Karagoz B, Yilmaz M, Bicak N, Arica MY (2011) Immobilization of catalase via adsorption on poly(styrene-d-glycidylmethacrylate) grafted and tetraethyldiethylene triamine ligand attached microbeads. Bioresour Technol 102:3653–3661

  10. 10.

    Demirbas O, Alkan M, Demirbas A (2013) Surface properties of catalase vand casein on kaolinite and design of experiments. Micropor Mesopor Mater 172:151–160

  11. 11.

    Bressani APP, Garcia KCA, Hirata DB, Mendes AA (2015) Production of alkyl esters from macaw palm oil by a sequential hydrolysis/esterification process using heterogeneous biocatalysts: optimization by response surface methodology. Bioprocess Biosyst Eng 38:287–297

  12. 12.

    Bayramoglu G, Arica MY (2012) Development of a sensitive method for selection of affinity ligand for trypsin using quartz crystal microbalance sensor. Bioprocess Biosyst Eng 35:423–431

  13. 13.

    Mohajershojaei K, Mahmoodi NM, Khosravi A (2015) Immobilization of laccase enzyme onto titania nanoparticle and decolorization of dyes from single and binary systems. Biotechnol Bioprocess Eng 20:109–116

  14. 14.

    Preety Hooda V (2014) Immobilization and kinetics of catalase on calcium carbonate nanoparticles attached epoxy support. Appl Biochem Biotechnol 172:115–130

  15. 15.

    Feng Q, Hou D, Zhao Y, Xu T, Menkhaus TJ, Fong H (2014) Electrospun regenerated cellulose nanofibrous membranes surface-grafted with polymer chains/brushes via the atom transfer radical polymerization method for catalase immobilization. ACS Appl Mater Interfaces 6:20958–20967

  16. 16.

    Feng Q, Zhao Y, Wei A, Li C, Wei Q, Fong H (2014) Immobilization of catalase on electrospun PVA/PA6−Cu(II) nanofibrous membrane for the development of efficient and reusable enzyme membrane reactor. Environ Sci Technol 48:10390–10397

  17. 17.

    Cowana DA, Fernandez-Lafuente R (2011) Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme Microb Technol 49:326–346

  18. 18.

    Bayramoglu G, Arica MY (2014) Activity and stability of urease entrapped in thermo-sensitive p(isopropylacrylamide-co-p(ethyleneglycole)-methacrylate) hydrogel. Bioprocess Biosyst Eng 37:235–243

  19. 19.

    Bayramoglu G, Altintas B, Arica MY (2012) Cross-linking of horseradish peroxidase adsorbed on polycationic films: utilization for direct dye degradation. Bioprocess Biosyst Eng 35:1355–1365

  20. 20.

    Yang D, Wang X, Shi J, Wang X, Zhang S, Han P, Jiang Z (2016) In situ synthesized rGO–Fe3O4 nanocomposites as enzyme immobilization support for achieving high activity recovery and easy recycling. Biochem Eng J 105:273–280

  21. 21.

    Zang J, Jia S, Liu Y, Wu S, Zhang Y (2012) A facile method to prepare chemically cross-linked and efficient polyvinyl alcohol/chitosan beads for catalase immobilization. Catal Commun 27:73–77

  22. 22.

    Li Y, Wang X-Y, Jiang X-P, Ye J-J, Zhang Y-W, Zhang X-Y (2015) Fabrication of graphene oxide decorated with Fe3O4@SiO2 for immobilization of cellulose. J Nanopart Res 17:8

  23. 23.

    Cengiz S, Cavas L, Yurdakoc K (2012) Bentonite and sepiolite as supporting media: immobilization of catalase. Appl Clay Sci 65–66:114–120

  24. 24.

    Bradford MM (1976) Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

  25. 25.

    Cetinus SA, Sahin E, Saraydin D (2009) Preparation of Cu(II) adsorbed chitosan beads for catalase immobilization. Food Chem 114:962–969

  26. 26.

    Chen N, Huang S, Liao XP, Shi B (2011) Immobilization of catalase by using Zr(IV)-modified collagen fiber as the supporting matrix. Process Biochem 46:2187–2193

  27. 27.

    Wang P, Qi C, Yu Y, Yuan J, Cui L, Tang G, Wang Q, Fan X (2015) Covalent immobilization of catalase onto regenerated silk fibroins via tyrosinase-catalyzed cross-linking. Appl Biochem Biotechnol 177:472–485

  28. 28.

    Feng Q, Wang Q, Tang B, Wie A, Wang X, Wie Q, Huang F, Cai Y, Hou D, Bi S (2013) Immobilization of catalases on amidoxime polyacrylonitrile nanofibrous membranes. Polym Int 62:251–256

  29. 29.

    Wang F, Guo C, Yang L-R, Liu C-Z (2013) Magnetic mesoporous silica nanoparticles: fabrication and their laccase immobilization performance. Bioresour Technol 101:8931–8935

  30. 30.

    Netto CGCM, Toma HE, Andrade LH (2013) Superparamagnetic nanoparticles as versatile carriers and supporting materials for enzymes. J Mol Catal B 85–86:71–92

  31. 31.

    Woo E-J, Kwon H-S, Lee C-H (2015) Preparation of nano-magnetite impregnated mesocellular foam composite with a Cu ligand for His-tagged enzyme immobilization. Chem Eng J 274:1–8

  32. 32.

    Romo-Sanchez S, Arevalo-Villena M, Romero EG, Ramirez HL, Perez AB (2014) Immobilization of β-glucosidase and its application for enhancement of aroma precursors in muscat wine. Food Bioprocess Technol 7:1381–1392

  33. 33.

    Wang Z-G, Ke B-B, Xu Z-K (2007) Covalent immobilization of redox enzyme on electrospun nonwoven poly(acrylonitrile-co-acrylic acid) nanofiber mesh filled with carbon nanotubes: a comprehensive study. Biotechnol Bioeng 97:708–720

  34. 34.

    Basak E, Aydemir T, Dincer A, Becerik SC (2013) Comperative study of catalase immobilization on chitosan, magnetic chitosan and chitosan-clay composite beads. Artif Cells Nanomed Biotechnol 41:408–413

  35. 35.

    Mateo C, Abian O, Fernandez-Lafuente R, Guisan JM (2000) Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment. Enzyme Microb Technol 26:509–515

  36. 36.

    Bayramoglu G, Akbulut A, Ozalp VC, Arica MY (2015) Immobilized lipase on microporous biosilica for enzymatic transesterification of algal oil. Chem Eng Res Design 95:12–21

  37. 37.

    Wu H, Liang Y, Shi J, Wang X, Yang D, Jiang Z (2013) Enhanced stability of catalase covalently immobilized on functionalized titania submicrospheres. Mater Sci Eng C 33:1438–1445

Download references

Author information

Correspondence to Gulay Bayramoglu.

Rights and permissions

Reprints and Permissions

About this article

Verify currency and authenticity via CrossMark

Cite this article

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

Download citation

Keywords

  • Michael addition
  • Surface modification
  • Catalase
  • Immobilized enzymes
  • Enzyme bioreactors