Immobilization of dextransucrase on functionalized TiO2 supports
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2018
Authors
Miljković, Miona G.Lazić, Vesna M.
Banjanac, Katarina
Davidović, Slađana Z.
Bezbradica, Dejan I.
Marinković, Aleksandar D.
Sredojević, Dušan
Nedeljković, Jovan
Dimitrijević-Branković, Suzana I.
Article (Published version)
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© 2018 Elsevier B.V.
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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:
dextransucrase / enzyme immobilization / surface functionalization of TiO2Source:
International Journal of Biological Macromolecules, 2018, 114, 1216-1223Funding / projects:
- Materials of Reduced Dimensions for Efficient Light Harvesting and Energy conversion (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-45020)
- Application of biotechnological methods for sustainable exploitation of by-products of agro-industry (RS-MESTD-Technological Development (TD or TR)-31035)
DOI: 10.1016/j.ijbiomac.2018.04.027
ISSN: 0141-8130; 1879-0003
PubMed: 29634963
WoS: 000435056900140
Scopus: 2-s2.0-85045236109
URI
http://linkinghub.elsevier.com/retrieve/pii/S0141813018302952https://vinar.vin.bg.ac.rs/handle/123456789/7776
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VinčaTY - JOUR AU - Miljković, Miona G. AU - Lazić, Vesna M. AU - Banjanac, Katarina AU - Davidović, Slađana Z. AU - Bezbradica, Dejan I. AU - Marinković, Aleksandar D. AU - Sredojević, Dušan AU - Nedeljković, Jovan AU - Dimitrijević-Branković, Suzana I. PY - 2018 UR - http://linkinghub.elsevier.com/retrieve/pii/S0141813018302952 UR - https://vinar.vin.bg.ac.rs/handle/123456789/7776 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%). T2 - International Journal of Biological Macromolecules T1 - Immobilization of dextransucrase on functionalized TiO2 supports VL - 114 SP - 1216 EP - 1223 DO - 10.1016/j.ijbiomac.2018.04.027 ER -
@article{ author = "Miljković, Miona G. and Lazić, Vesna M. and Banjanac, Katarina and Davidović, Slađana Z. and Bezbradica, Dejan I. and Marinković, Aleksandar D. and Sredojević, Dušan and Nedeljković, Jovan and Dimitrijević-Branković, Suzana I.", 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%).", journal = "International Journal of Biological Macromolecules", title = "Immobilization of dextransucrase on functionalized TiO2 supports", volume = "114", pages = "1216-1223", doi = "10.1016/j.ijbiomac.2018.04.027" }
Miljković, M. G., Lazić, V. M., Banjanac, K., Davidović, S. Z., Bezbradica, D. I., Marinković, A. D., Sredojević, D., Nedeljković, J.,& Dimitrijević-Branković, S. I.. (2018). Immobilization of dextransucrase on functionalized TiO2 supports. in International Journal of Biological Macromolecules, 114, 1216-1223. https://doi.org/10.1016/j.ijbiomac.2018.04.027
Miljković MG, Lazić VM, Banjanac K, Davidović SZ, Bezbradica DI, Marinković AD, Sredojević D, Nedeljković J, Dimitrijević-Branković SI. 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 G., Lazić, Vesna M., Banjanac, Katarina, Davidović, Slađana Z., Bezbradica, Dejan I., Marinković, Aleksandar D., Sredojević, Dušan, Nedeljković, Jovan, Dimitrijević-Branković, Suzana I., "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 . .