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Immobilization of dextransucrase on functionalized TiO2 supports

Authorized Users Only
2018
Authors
Miljković, Miona
Lazić, Vesna M.
Banjanac, Katarina
Davidović, Slađana
Bezbradica, Dejan
Marinković, Aleksandar
Sredojević, Dušan
Nedeljković, Jovan
Dimitrijević-Branković, Suzana
Article (Published version)
Metadata
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Abstract
The TiO2 based hybrid supports with different functional groups (amino, glutaraldehyde or epoxy) were prepared and their influence on immobilization of dextransucrase (DS) was studied. Novel synthetic route for surface modification of TiO2 with amino and glutaraldehyde groups was developed taking advantage of charge transfer complex (CTC) formation between surface Ti atoms and salicylate-type of ligand (5 aminosalicylic acid (5-ASA)). The proposed coordination of 5-ASA to the surface of TiO2 powder and optical properties of CTC was presented. The pristine TiO2 and amino functionalized TiO2 have higher sorption capacity for DS (12.6 and 12.0 mg g(-1), respectively) compared to glutaraldehyde and epoxy activated supports (9.6 and 9.8 mg g(-1) respectively). However, immobilized enzyme to either glutaraldehyde or epoxy functionalized TiO2 have almost two times higher expressed activities compared to pristine TiO2 support (258, 235 and 142 IU g(-1), respectively). Thermal stability of enzy...me immobilized on glutaraldehyde and epoxy functionalized supports was studied at 40 degrees C, as well as operational stability under long-run working conditions in repeated cycles. After five cycles, DS imobilized on glutaraldehyde activated support retained almost 70% of its initial expressed activity, while, after five cycles, performance of DS immobilized on epoxy activated support was significantly lower (15%).

Keywords:
Surface functionalization of TiO2 / Dextransucrase / Enzyme immobilization
Source:
International Journal of Biological Macromolecules, 2018, 114, 1216-1223
Publisher:
  • Elsevier Science Bv, Amsterdam
Funding / projects:
  • Materials of Reduced Dimensions for Efficient Light Harvesting and Energy conversion (RS-45020)
  • Application of biotechnological methods for sustainable exploitation of by-products of agro-industry (RS-31035)

DOI: 10.1016/j.ijbiomac.2018.04.027

ISSN: 0141-8130

PubMed: 29634963

WoS: 000435056900140

Scopus: 2-s2.0-85045236109
[ Google Scholar ]
14
12
URI
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4014
Collections
  • Radovi istraživača / Researchers’ publications (TMF)
  • Radovi istraživača (Inovacioni centar) / Researchers’ publications (Innovation Centre)
Institution/Community
Tehnološko-metalurški fakultet
TY  - JOUR
AU  - Miljković, Miona
AU  - Lazić, Vesna M.
AU  - Banjanac, Katarina
AU  - Davidović, Slađana
AU  - Bezbradica, Dejan
AU  - Marinković, Aleksandar
AU  - Sredojević, Dušan
AU  - Nedeljković, Jovan
AU  - Dimitrijević-Branković, Suzana
PY  - 2018
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4014
AB  - The TiO2 based hybrid supports with different functional groups (amino, glutaraldehyde or epoxy) were prepared and their influence on immobilization of dextransucrase (DS) was studied. Novel synthetic route for surface modification of TiO2 with amino and glutaraldehyde groups was developed taking advantage of charge transfer complex (CTC) formation between surface Ti atoms and salicylate-type of ligand (5 aminosalicylic acid (5-ASA)). The proposed coordination of 5-ASA to the surface of TiO2 powder and optical properties of CTC was presented. The pristine TiO2 and amino functionalized TiO2 have higher sorption capacity for DS (12.6 and 12.0 mg g(-1), respectively) compared to glutaraldehyde and epoxy activated supports (9.6 and 9.8 mg g(-1) respectively). However, immobilized enzyme to either glutaraldehyde or epoxy functionalized TiO2 have almost two times higher expressed activities compared to pristine TiO2 support (258, 235 and 142 IU g(-1), respectively). Thermal stability of enzyme immobilized on glutaraldehyde and epoxy functionalized supports was studied at 40 degrees C, as well as operational stability under long-run working conditions in repeated cycles. After five cycles, DS imobilized on glutaraldehyde activated support retained almost 70% of its initial expressed activity, while, after five cycles, performance of DS immobilized on epoxy activated support was significantly lower (15%).
PB  - Elsevier Science Bv, Amsterdam
T2  - International Journal of Biological Macromolecules
T1  - Immobilization of dextransucrase on functionalized TiO2 supports
EP  - 1223
SP  - 1216
VL  - 114
DO  - 10.1016/j.ijbiomac.2018.04.027
ER  - 
@article{
author = "Miljković, Miona and Lazić, Vesna M. and Banjanac, Katarina and Davidović, Slađana and Bezbradica, Dejan and Marinković, Aleksandar and Sredojević, Dušan and Nedeljković, Jovan and Dimitrijević-Branković, Suzana",
year = "2018",
abstract = "The TiO2 based hybrid supports with different functional groups (amino, glutaraldehyde or epoxy) were prepared and their influence on immobilization of dextransucrase (DS) was studied. Novel synthetic route for surface modification of TiO2 with amino and glutaraldehyde groups was developed taking advantage of charge transfer complex (CTC) formation between surface Ti atoms and salicylate-type of ligand (5 aminosalicylic acid (5-ASA)). The proposed coordination of 5-ASA to the surface of TiO2 powder and optical properties of CTC was presented. The pristine TiO2 and amino functionalized TiO2 have higher sorption capacity for DS (12.6 and 12.0 mg g(-1), respectively) compared to glutaraldehyde and epoxy activated supports (9.6 and 9.8 mg g(-1) respectively). However, immobilized enzyme to either glutaraldehyde or epoxy functionalized TiO2 have almost two times higher expressed activities compared to pristine TiO2 support (258, 235 and 142 IU g(-1), respectively). Thermal stability of enzyme immobilized on glutaraldehyde and epoxy functionalized supports was studied at 40 degrees C, as well as operational stability under long-run working conditions in repeated cycles. After five cycles, DS imobilized on glutaraldehyde activated support retained almost 70% of its initial expressed activity, while, after five cycles, performance of DS immobilized on epoxy activated support was significantly lower (15%).",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "International Journal of Biological Macromolecules",
title = "Immobilization of dextransucrase on functionalized TiO2 supports",
pages = "1223-1216",
volume = "114",
doi = "10.1016/j.ijbiomac.2018.04.027"
}
Miljković, M., Lazić, V. M., Banjanac, K., Davidović, S., Bezbradica, D., Marinković, A., Sredojević, D., Nedeljković, J.,& Dimitrijević-Branković, S.. (2018). Immobilization of dextransucrase on functionalized TiO2 supports. in International Journal of Biological Macromolecules
Elsevier Science Bv, Amsterdam., 114, 1216-1223.
https://doi.org/10.1016/j.ijbiomac.2018.04.027
Miljković M, Lazić VM, Banjanac K, Davidović S, Bezbradica D, Marinković A, Sredojević D, Nedeljković J, Dimitrijević-Branković S. Immobilization of dextransucrase on functionalized TiO2 supports. in International Journal of Biological Macromolecules. 2018;114:1216-1223.
doi:10.1016/j.ijbiomac.2018.04.027 .
Miljković, Miona, Lazić, Vesna M., Banjanac, Katarina, Davidović, Slađana, Bezbradica, Dejan, Marinković, Aleksandar, Sredojević, Dušan, Nedeljković, Jovan, Dimitrijević-Branković, Suzana, "Immobilization of dextransucrase on functionalized TiO2 supports" in International Journal of Biological Macromolecules, 114 (2018):1216-1223,
https://doi.org/10.1016/j.ijbiomac.2018.04.027 . .

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