Immobilization of dextransucrase on functionalized TiO2 supports
Само за регистроване кориснике
2018
Аутори
Miljković, MionaLazić, Vesna M.
Banjanac, Katarina
Davidović, Slađana
Bezbradica, Dejan
Marinković, Aleksandar
Sredojević, Dušan
Nedeljković, Jovan
Dimitrijević-Branković, Suzana
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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%).
Кључне речи:
Surface functionalization of TiO2 / Dextransucrase / Enzyme immobilizationИзвор:
International Journal of Biological Macromolecules, 2018, 114, 1216-1223Издавач:
- Elsevier Science Bv, Amsterdam
Финансирање / пројекти:
- Материјали редуковане димензионалности за ефикасну апсорпцију светлости и конверзију енергије (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-45020)
- Примена биотехнолошких метода у одрживом искоришћењу нус-производа агроиндустрије (RS-MESTD-Technological Development (TD or TR)-31035)
DOI: 10.1016/j.ijbiomac.2018.04.027
ISSN: 0141-8130
PubMed: 29634963
WoS: 000435056900140
Scopus: 2-s2.0-85045236109
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - 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 . .