The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media
Authors
Izrael-Živković, LidijaŽivković, Ljiljana S.
Beškoski, Vladimir
Gopčević, Kristina
Jokić, Bojan
Radosavljević, Dragoslav S.
Karadžić, Ivanka M.
Article (Accepted Version)
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The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic... constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.
Keywords:
Candida rugosa lipase / Cyclohexane / Degussa P25 titania / Immobilization / Kinetic parametersSource:
Journal of Molecular Catalysis. B: Enzymatic, 2016, 133Funding / projects:
- Simultaneous Bioremediation and Soilification of Degraded Areas to Preserve Natural Resources of Biologically Active Substances, and Development and Production of Biomaterials and Dietetic Products (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-43004)
- Govorna komunikacija čovek-mašina (RS-MESTD-MPN2006-2010-11001)
Note:
- This is peer-reviewed version of the following article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3649
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Izrael-Živković, Lidija AU - Živković, Ljiljana S. AU - Beškoski, Vladimir AU - Gopčević, Kristina AU - Jokić, Bojan AU - Radosavljević, Dragoslav S. AU - Karadžić, Ivanka M. PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3648 AB - The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V. T2 - Journal of Molecular Catalysis. B: Enzymatic T1 - The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media VL - 133 DO - 10.1016/j.molcatb.2017.06.001 ER -
@article{ author = "Izrael-Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Jokić, Bojan and Radosavljević, Dragoslav S. and Karadžić, Ivanka M.", year = "2016", abstract = "The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.", journal = "Journal of Molecular Catalysis. B: Enzymatic", title = "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media", volume = "133", doi = "10.1016/j.molcatb.2017.06.001" }
Izrael-Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Jokić, B., Radosavljević, D. S.,& Karadžić, I. M.. (2016). The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic, 133. https://doi.org/10.1016/j.molcatb.2017.06.001
Izrael-Živković L, Živković LS, Beškoski V, Gopčević K, Jokić B, Radosavljević DS, Karadžić IM. The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media. in Journal of Molecular Catalysis. B: Enzymatic. 2016;133. doi:10.1016/j.molcatb.2017.06.001 .
Izrael-Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Jokić, Bojan, Radosavljević, Dragoslav S., Karadžić, Ivanka M., "The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media" in Journal of Molecular Catalysis. B: Enzymatic, 133 (2016), https://doi.org/10.1016/j.molcatb.2017.06.001 . .