TY  - JOUR
AU  - Izrael-Živković, Lidija T.
AU  - Živković, Ljiljana
AU  - Jokić, Bojan M.
AU  - Savić, Andrija B.
AU  - Karadzic, Ivanka M.
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/796
AB  - The impact of the surface charge of alumina supports on the adsorption of Candida rugosa lipase was investigated in terms of the zeta potentials of the adsorption partners. The lipase adhered onto alumina with similar efficiency under both repulsive and attractive electrostatic conditions, shifting the zeta potential of the support towards that of the enzyme. The behavior was explained by a heterogeneous distribution of the surface charge of the lipase molecule. Special emphasis in this study was placed on the effect of immobilization on the enzyme kinetics and principal reasons for enzyme immobilization: improvement in stability and potential for reuse. The enzyme affinity was not altered by its adsorption onto alumina, while the Vmax value of the lipase decreased. The thermostability of the adsorbed lipase was improved. A significant potential for reuse was found.
T2  - Journal of the Serbian Chemical Society
T1  - Adsorption of Candida rugosa lipase onto alumina: effect of surface charge
VL  - 80
IS  - 9
SP  - 1113
EP  - 1125
DO  - 10.2298/JSC150222035I
ER  - 

@article{
author = "Izrael-Živković, Lidija T. and Živković, Ljiljana and Jokić, Bojan M. and Savić, Andrija B. and Karadzic, Ivanka M.",
year = "2015",
abstract = "The impact of the surface charge of alumina supports on the adsorption of Candida rugosa lipase was investigated in terms of the zeta potentials of the adsorption partners. The lipase adhered onto alumina with similar efficiency under both repulsive and attractive electrostatic conditions, shifting the zeta potential of the support towards that of the enzyme. The behavior was explained by a heterogeneous distribution of the surface charge of the lipase molecule. Special emphasis in this study was placed on the effect of immobilization on the enzyme kinetics and principal reasons for enzyme immobilization: improvement in stability and potential for reuse. The enzyme affinity was not altered by its adsorption onto alumina, while the Vmax value of the lipase decreased. The thermostability of the adsorbed lipase was improved. A significant potential for reuse was found.",
journal = "Journal of the Serbian Chemical Society",
title = "Adsorption of Candida rugosa lipase onto alumina: effect of surface charge",
volume = "80",
number = "9",
pages = "1113-1125",
doi = "10.2298/JSC150222035I"
}

Izrael-Živković, L. T., Živković, L., Jokić, B. M., Savić, A. B.,& Karadzic, I. M.. (2015). Adsorption of Candida rugosa lipase onto alumina: effect of surface charge. in Journal of the Serbian Chemical Society, 80(9), 1113-1125.
https://doi.org/10.2298/JSC150222035I

Izrael-Živković LT, Živković L, Jokić BM, Savić AB, Karadzic IM. Adsorption of Candida rugosa lipase onto alumina: effect of surface charge. in Journal of the Serbian Chemical Society. 2015;80(9):1113-1125.
doi:10.2298/JSC150222035I .

Izrael-Živković, Lidija T., Živković, Ljiljana, Jokić, Bojan M., Savić, Andrija B., Karadzic, Ivanka M., "Adsorption of Candida rugosa lipase onto alumina: effect of surface charge" in Journal of the Serbian Chemical Society, 80, no. 9 (2015):1113-1125,
https://doi.org/10.2298/JSC150222035I . .

TY  - JOUR
AU  - Izrael-Živković, Lidija T.
AU  - Živković, Ljiljana
AU  - Babić, Biljana M.
AU  - Kokunešoski, Maja
AU  - Jokić, Bojan M.
AU  - Karadzic, Ivanka M.
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/336
AB  - Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica SBA-15 and zirconia. The adsorption process was studied as a function of pH in terms of percent of adsorbed lipase, enzyme activity and zeta potential of support and enzyme. Several analytical approaches such as laser Doppler electrophoresis, Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that the lipase was successfully immobilized onto both supports. The zeta-potential data suggest that the adsorption efficiency does not depends on the sign but on the magnitude of the surface charge of adsorption partners, and therefore underline the importance of their dispersion stability. Adsorption to material surface altered enzyme characteristics. nu(max), for the lipase immobilized onto silica and zirconia were 4.8-fold and 3.6-fold lower than that of the free lipase, respectively. The Km showed no alteration of enzyme-substrate affinity on zirconia support, whereas the enzyme immobilized on silica had 3.6 times lower affinity. Thermostability at 60 degrees C of the lipase was improved 12-fold on zirconia and 4-fold on silica. Finally, in examining reusability, the immobilized lipase retained more than 90% of initial activity after eight reuses on both supports. (C) 2014 Elsevier B.V. All rights reserved.
T2  - Biochemical Engineering Journal
T1  - Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia
VL  - 93
SP  - 73
EP  - 83
DO  - 10.1016/j.bej.2014.09.012
ER  - 

@article{
author = "Izrael-Živković, Lidija T. and Živković, Ljiljana and Babić, Biljana M. and Kokunešoski, Maja and Jokić, Bojan M. and Karadzic, Ivanka M.",
year = "2015",
abstract = "Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica SBA-15 and zirconia. The adsorption process was studied as a function of pH in terms of percent of adsorbed lipase, enzyme activity and zeta potential of support and enzyme. Several analytical approaches such as laser Doppler electrophoresis, Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that the lipase was successfully immobilized onto both supports. The zeta-potential data suggest that the adsorption efficiency does not depends on the sign but on the magnitude of the surface charge of adsorption partners, and therefore underline the importance of their dispersion stability. Adsorption to material surface altered enzyme characteristics. nu(max), for the lipase immobilized onto silica and zirconia were 4.8-fold and 3.6-fold lower than that of the free lipase, respectively. The Km showed no alteration of enzyme-substrate affinity on zirconia support, whereas the enzyme immobilized on silica had 3.6 times lower affinity. Thermostability at 60 degrees C of the lipase was improved 12-fold on zirconia and 4-fold on silica. Finally, in examining reusability, the immobilized lipase retained more than 90% of initial activity after eight reuses on both supports. (C) 2014 Elsevier B.V. All rights reserved.",
journal = "Biochemical Engineering Journal",
title = "Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia",
volume = "93",
pages = "73-83",
doi = "10.1016/j.bej.2014.09.012"
}

Izrael-Živković, L. T., Živković, L., Babić, B. M., Kokunešoski, M., Jokić, B. M.,& Karadzic, I. M.. (2015). Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia. in Biochemical Engineering Journal, 93, 73-83.
https://doi.org/10.1016/j.bej.2014.09.012

Izrael-Živković LT, Živković L, Babić BM, Kokunešoski M, Jokić BM, Karadzic IM. Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia. in Biochemical Engineering Journal. 2015;93:73-83.
doi:10.1016/j.bej.2014.09.012 .

Izrael-Živković, Lidija T., Živković, Ljiljana, Babić, Biljana M., Kokunešoski, Maja, Jokić, Bojan M., Karadzic, Ivanka M., "Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia" in Biochemical Engineering Journal, 93 (2015):73-83,
https://doi.org/10.1016/j.bej.2014.09.012 . .