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Immobilization of Catalase onto Polylysine Modified Chitosan Polymer

Yıl 2021, Cilt: 6 Sayı: 3, 208 - 217, 15.12.2021
https://doi.org/10.28978/nesciences.1036851

Öz

In this study, chitosan polymer was modified in two different ways and used for the immobilization of bovine liver catalase (CAT). First, it was activated with glutaraldehyde (GAL), and then covalently immobilized covalently onto the support via lysine amino acid residue in CAT. In the second modification, GAL-activated chitosan was interacted with polylysine (pLYS), then reactivated with GAL and used in CAT immobilization. Samples of bare chitosan (Chi), GAL-activated (ChiGAL), polylysine-modified (ChiGAL-pLYS), reactivated with GAL (ChiGAL-pLYSGAL) and CAT-immobilized chitosan (ChiGAL -CAT and ChiGAL-pLYSGAL-CAT) were all characterized by FTIR. The enzymatic activities of Free CAT, ChiGAL -CAT and ChiGAL-pLYSGAL-CAT samples were investigated at different pH and temperatures and the values with the highest activity were determined. In addition, the effect of substrate concentration on activity under optimal conditions was investigated. Optimum pH values of Free CAT, ChiGAL-CAT and ChiGAL-pLYSGAL-CAT samples were 7.5, 7.0 and 7.0, respectively; temperature values were determined as 25, 30 and 35 C, respectively. After immobilization, the Vmax values of the enzymes decreased, the Km values increased, and the efficiency of catalase immobilized to the polylysine modified support was found to be higher. It was observed that after 20 repeatedly use in the column reactor, ChiGAL-CAT and ChiGAL-pLYSGAL-CAT enzymes retained 88 % and 76 % of their initial activities, respectively.

Kaynakça

  • Alptekin, O., Tükel S.S, Yıldırım D., & Alagöz, D. (2010) Immobilization of catalase onto Eupergit C and its characterization. Journal of Molecular Catalysis B: Enzymatic. 64, 177-183. https://doi.org/10.1016/j.molcatb.2009.09.010.
  • Arabacı, G. & Usluoglu, A. (2012). Immobilization of dill (Anethum Graveolens L.) catalase and its properties. Asia-Pacific Journal of Chemical Engineering. 7, S296-S300. https://doi.org/10.1002/apj.1647.
  • Barreca, D., Neri, G., Scala, A., Fazio, E., Gentile, D., Rescifina, A.& Piperno, A. (2018). Covalently immobilzed catalase on functionalized graphene: effect on the activity, immobilization efficiency, and tetramer stability. Biomaterials Science. 6, 3231. https://doi.org/10.1039/C8BM00850G.
  • Başak, E., 2011. Immobilization of catalase enzyme on modified chitosan beads. MSci Thesis,. Celal Bayar University, 53s, Manisa, Turkey.
  • Bayramoglu, G., Karagoz B., Yilmaz M., Bicak N., Arica M.Y. (2011). Immobilization of catalase via adsorption on poly (styrene-d-glycidylmethacrylate grafted and tetraethyldiethylenetriamine ligand attached microbeads. Bioresource Technology, 102, 3653-3661. https://doi.org/10.1016/j.biortech.2010.12.029.
  • Bayramoglu, G., Arica, M.Y., Genc, A., Ozalp, V.C., Ince, A. & Bicak N. (2016). A facile and efficient method of enzyme immobilization on silica particles via Michael acceptor film coatings: immobilized catalase in a plug flow reactor. Bioprocess and Biosystem Engineering. 39, 871-881. https://doi.org/10.1007/s00449-016-1566-0.
  • Collins, S.E., Lassale, V. & Ferreira, M.L. (2011). FTIR-ATR characterization of free Rhizomucor meihei lipase (RML), lipozyme RM IM and chitosan-immobilized RML. Journal of Molecular Catalysis B: Enzymatic. 72, 220-228. https://doi.org/10.1016/j.molcatb.2011.06.009.
  • Çetinus, Ş. A., Öztop, H. N. & Saraydın, D., (2007). Immobilization of catalase onto chitosan and cibacron blue F3GA attached chitosan beads. Enzyme and Microbial Technology, 41: 447–454. https://doi.org/10.1016/j.enzmictec.2007.03.014.
  • Çorman, M.E:, Öztürk, N., Tüzmen, N., Akgöl, S. & Denizli A. (2010). Magnetic polymeric nanospheres as an immobilized metal affinity chromatography (IMAC) support for catalase. Biochemical Engineering Journal, 49, 159-164. https://doi.org/10.1016/j.bej.2009.11.002.
  • Ozyilmaz, G., Tukel, S.S. & Alptekin, O., (2005) Activity and storage stability of immobilized glucose oxidase onto magnesium silicate. Journal of Molecular Catalysis B: Enzymatic, 35: 154-160. https://doi.org/10.1016/j.molcatb.2005.07.001.
  • Ozyilmaz, G., Tukel, S.S. & Alptekin O., (2007). Kinetic properties and storage stability of catalase immobilized on to florisil. Indian Journal of Biochemistry & Biophysics, 44, 38-43
  • Sel, E., Ulu, A., Ateş, B. & Köytepe S. (2021). Comparative study of catalase immobilization via adsorption on P(MMA-co-PEG500MA) structures as an effectice polymer support. Polymer Bulletin, 78, 2663-2684. https://doi.org/10.1007/s00289-020-03233-0.
  • Seriner, R.(2010). Purification of catalase enzyme from cucumber (Cucimus sativus). MSci Thesis. Çukurova Üniversitesi, 45s, Adana.
  • Shentu, J., Wu, J., Song, W. & Jia, Z., (2005). Chitosan microspheres as immobilized dye affinity support for catalase adsorption. International Journal of Biological Macromolecules, 37, 42–46. https://doi.org/10.1016/j.ijbiomac.2005.08.004.
  • Silvana, T., Gemelli, S., Segalin, J., & Brandelli, A. (2012). Immobilization of keratinolytic metalloprotease from Chryseobacterium sp. Strain kr6 on glutaraldehyde-activated chitosan. Journal of Microbiology and Biotechnology, 22, 818–825. https://doi.org/10.4014/jmb.1111.11048.
  • Tukel, S. S. & Alptekin, O., (2004). Immobilization and kinetics of catalase onto magnesium silicate. Process Biochemistry, 39, 2149–2155. https://doi.org/10.1016/j.procbio.2003.11.010.
  • Yıldırım, E., (2010). Activity and kinetics of catalase enzyme in saline soils. MSci Thesis,. Selçuk University, 81s, Konya.
Yıl 2021, Cilt: 6 Sayı: 3, 208 - 217, 15.12.2021
https://doi.org/10.28978/nesciences.1036851

Öz

Kaynakça

  • Alptekin, O., Tükel S.S, Yıldırım D., & Alagöz, D. (2010) Immobilization of catalase onto Eupergit C and its characterization. Journal of Molecular Catalysis B: Enzymatic. 64, 177-183. https://doi.org/10.1016/j.molcatb.2009.09.010.
  • Arabacı, G. & Usluoglu, A. (2012). Immobilization of dill (Anethum Graveolens L.) catalase and its properties. Asia-Pacific Journal of Chemical Engineering. 7, S296-S300. https://doi.org/10.1002/apj.1647.
  • Barreca, D., Neri, G., Scala, A., Fazio, E., Gentile, D., Rescifina, A.& Piperno, A. (2018). Covalently immobilzed catalase on functionalized graphene: effect on the activity, immobilization efficiency, and tetramer stability. Biomaterials Science. 6, 3231. https://doi.org/10.1039/C8BM00850G.
  • Başak, E., 2011. Immobilization of catalase enzyme on modified chitosan beads. MSci Thesis,. Celal Bayar University, 53s, Manisa, Turkey.
  • Bayramoglu, G., Karagoz B., Yilmaz M., Bicak N., Arica M.Y. (2011). Immobilization of catalase via adsorption on poly (styrene-d-glycidylmethacrylate grafted and tetraethyldiethylenetriamine ligand attached microbeads. Bioresource Technology, 102, 3653-3661. https://doi.org/10.1016/j.biortech.2010.12.029.
  • Bayramoglu, G., Arica, M.Y., Genc, A., Ozalp, V.C., Ince, A. & Bicak N. (2016). A facile and efficient method of enzyme immobilization on silica particles via Michael acceptor film coatings: immobilized catalase in a plug flow reactor. Bioprocess and Biosystem Engineering. 39, 871-881. https://doi.org/10.1007/s00449-016-1566-0.
  • Collins, S.E., Lassale, V. & Ferreira, M.L. (2011). FTIR-ATR characterization of free Rhizomucor meihei lipase (RML), lipozyme RM IM and chitosan-immobilized RML. Journal of Molecular Catalysis B: Enzymatic. 72, 220-228. https://doi.org/10.1016/j.molcatb.2011.06.009.
  • Çetinus, Ş. A., Öztop, H. N. & Saraydın, D., (2007). Immobilization of catalase onto chitosan and cibacron blue F3GA attached chitosan beads. Enzyme and Microbial Technology, 41: 447–454. https://doi.org/10.1016/j.enzmictec.2007.03.014.
  • Çorman, M.E:, Öztürk, N., Tüzmen, N., Akgöl, S. & Denizli A. (2010). Magnetic polymeric nanospheres as an immobilized metal affinity chromatography (IMAC) support for catalase. Biochemical Engineering Journal, 49, 159-164. https://doi.org/10.1016/j.bej.2009.11.002.
  • Ozyilmaz, G., Tukel, S.S. & Alptekin, O., (2005) Activity and storage stability of immobilized glucose oxidase onto magnesium silicate. Journal of Molecular Catalysis B: Enzymatic, 35: 154-160. https://doi.org/10.1016/j.molcatb.2005.07.001.
  • Ozyilmaz, G., Tukel, S.S. & Alptekin O., (2007). Kinetic properties and storage stability of catalase immobilized on to florisil. Indian Journal of Biochemistry & Biophysics, 44, 38-43
  • Sel, E., Ulu, A., Ateş, B. & Köytepe S. (2021). Comparative study of catalase immobilization via adsorption on P(MMA-co-PEG500MA) structures as an effectice polymer support. Polymer Bulletin, 78, 2663-2684. https://doi.org/10.1007/s00289-020-03233-0.
  • Seriner, R.(2010). Purification of catalase enzyme from cucumber (Cucimus sativus). MSci Thesis. Çukurova Üniversitesi, 45s, Adana.
  • Shentu, J., Wu, J., Song, W. & Jia, Z., (2005). Chitosan microspheres as immobilized dye affinity support for catalase adsorption. International Journal of Biological Macromolecules, 37, 42–46. https://doi.org/10.1016/j.ijbiomac.2005.08.004.
  • Silvana, T., Gemelli, S., Segalin, J., & Brandelli, A. (2012). Immobilization of keratinolytic metalloprotease from Chryseobacterium sp. Strain kr6 on glutaraldehyde-activated chitosan. Journal of Microbiology and Biotechnology, 22, 818–825. https://doi.org/10.4014/jmb.1111.11048.
  • Tukel, S. S. & Alptekin, O., (2004). Immobilization and kinetics of catalase onto magnesium silicate. Process Biochemistry, 39, 2149–2155. https://doi.org/10.1016/j.procbio.2003.11.010.
  • Yıldırım, E., (2010). Activity and kinetics of catalase enzyme in saline soils. MSci Thesis,. Selçuk University, 81s, Konya.
Toplam 17 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Yapısal Biyoloji
Bölüm 1
Yazarlar

Gül Ozyılmaz Bu kişi benim 0000-0002-1868-8611

Yayımlanma Tarihi 15 Aralık 2021
Gönderilme Tarihi 1 Mart 2021
Yayımlandığı Sayı Yıl 2021 Cilt: 6 Sayı: 3

Kaynak Göster

APA Ozyılmaz, G. (2021). Immobilization of Catalase onto Polylysine Modified Chitosan Polymer. Natural and Engineering Sciences, 6(3), 208-217. https://doi.org/10.28978/nesciences.1036851

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