Radosavljević, Dragoslav S.

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  • Radosavljević, Dragoslav S. (3)
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Supplementary data for the 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

Izrael-Živković, Lidija; Živković, Ljiljana S.; Beškoski, Vladimir; Gopčević, Kristina; Jokić, Bojan; Radosavljević, Dragoslav S.; Karadžić, Ivanka M.

(2016)

TY  - DATA
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/123456789/3649
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Supplementary data for the 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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3649
ER  - 
@misc{
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",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Supplementary data for the 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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3649"
}
Izrael-Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Jokić, B., Radosavljević, D. S.,& Karadžić, I. M.. (2016). Supplementary data for the 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. in Journal of Molecular Catalysis. B: Enzymatic.
https://hdl.handle.net/21.15107/rcub_cherry_3649
Izrael-Živković L, Živković LS, Beškoski V, Gopčević K, Jokić B, Radosavljević DS, Karadžić IM. Supplementary data for the 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. in Journal of Molecular Catalysis. B: Enzymatic. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3649 .
Izrael-Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Jokić, Bojan, Radosavljević, Dragoslav S., Karadžić, Ivanka M., "Supplementary data for the 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" in Journal of Molecular Catalysis. B: Enzymatic (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3649 .

The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media

Izrael-Živković, Lidija; Živković, Ljiljana S.; Beškoski, Vladimir; Gopčević, Kristina; Jokić, Bojan; Radosavljević, Dragoslav S.; Karadžić, Ivanka M.

(2016)

TY  - 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 . .
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The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media

Izrael-Živković, Lidija; Živković, Ljiljana S.; Beškoski, Vladimir; Gopčević, Kristina; Jokić, Bojan; Radosavljević, Dragoslav S.; Karadžić, Ivanka M.

(2016)

TY  - 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/123456789/315
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 . .
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