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  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5843
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 . .

TY  - JOUR
AU  - Grbavčić, Sanja
AU  - Marković, Darka
AU  - Rajilić-Stojanović, Mirjana
AU  - Antov, Mirjana
AU  - Sciban, Marina
AU  - Karadžić, Ivanka
AU  - Knežević-Jugović, Zorica
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2977
AB  - A lipase derived from an indigenous extremophile Pseudomonas aeruginosa strain isolated from rancid metalworking fluid was evaluated as a detergent additive. Applicability of the obtained enzyme as an additive in detergent formulations was confirmed by its implementation in the formulations of several new products differing in surfactant type and concentrations, demonstrating satisfactory performance in terms of degreasing efficiency and composition of the washing wastewater. The degreasing efficiency of different enzyme-containing detergent formulations was studied on cotton fabric samples stained with triolein and compared to that of formulations containing only surfactant. The highest efficiency of the fatty soil removal in formulations with a low content of surfactants (0.4 %) was noted in the enzyme formulation containing Lutensol(A (R)) XP-80 (degreasing efficiency  gt  80 %) and Triton(A (R)) X-100 (degreasing efficiency  gt  60 %). An attempt was then made to optimize the composition of the enzyme formulation on the basis of one or both of these surfactants using statistically planned experiments and response surface methodology (RSM). Taking into consideration the environmental aspects and the shown detergency, it appeared that rather high degreasing effects were achieved in formulations based on a low quantities of Lutensol(A (R)) XP-80 (0.4 %) at all pH values. However, pH seemed to have a notable effect since the degreasing efficiency significantly increased with increasing pH and the amount of the enzyme. Formulations having a moderate alkaline pH profile and higher amount of enzyme exhibited a high cleaning performance of fatty soil even at a low concentration of the surfactant.
PB  - Wiley, Hoboken
T2  - Journal of Surfactants and Detergents
T1  - Development of an Environmentally Acceptable Detergent Formulation for Fatty Soils Based on the Lipase from the Indigenous Extremophile Pseudomonas aeruginosa Strain
EP  - 395
IS  - 3
SP  - 383
VL  - 18
DO  - 10.1007/s11743-015-1674-x
ER  - 

@article{
author = "Grbavčić, Sanja and Marković, Darka and Rajilić-Stojanović, Mirjana and Antov, Mirjana and Sciban, Marina and Karadžić, Ivanka and Knežević-Jugović, Zorica",
year = "2015",
abstract = "A lipase derived from an indigenous extremophile Pseudomonas aeruginosa strain isolated from rancid metalworking fluid was evaluated as a detergent additive. Applicability of the obtained enzyme as an additive in detergent formulations was confirmed by its implementation in the formulations of several new products differing in surfactant type and concentrations, demonstrating satisfactory performance in terms of degreasing efficiency and composition of the washing wastewater. The degreasing efficiency of different enzyme-containing detergent formulations was studied on cotton fabric samples stained with triolein and compared to that of formulations containing only surfactant. The highest efficiency of the fatty soil removal in formulations with a low content of surfactants (0.4 %) was noted in the enzyme formulation containing Lutensol(A (R)) XP-80 (degreasing efficiency  gt  80 %) and Triton(A (R)) X-100 (degreasing efficiency  gt  60 %). An attempt was then made to optimize the composition of the enzyme formulation on the basis of one or both of these surfactants using statistically planned experiments and response surface methodology (RSM). Taking into consideration the environmental aspects and the shown detergency, it appeared that rather high degreasing effects were achieved in formulations based on a low quantities of Lutensol(A (R)) XP-80 (0.4 %) at all pH values. However, pH seemed to have a notable effect since the degreasing efficiency significantly increased with increasing pH and the amount of the enzyme. Formulations having a moderate alkaline pH profile and higher amount of enzyme exhibited a high cleaning performance of fatty soil even at a low concentration of the surfactant.",
publisher = "Wiley, Hoboken",
journal = "Journal of Surfactants and Detergents",
title = "Development of an Environmentally Acceptable Detergent Formulation for Fatty Soils Based on the Lipase from the Indigenous Extremophile Pseudomonas aeruginosa Strain",
pages = "395-383",
number = "3",
volume = "18",
doi = "10.1007/s11743-015-1674-x"
}

Grbavčić, S., Marković, D., Rajilić-Stojanović, M., Antov, M., Sciban, M., Karadžić, I.,& Knežević-Jugović, Z.. (2015). Development of an Environmentally Acceptable Detergent Formulation for Fatty Soils Based on the Lipase from the Indigenous Extremophile Pseudomonas aeruginosa Strain. in Journal of Surfactants and Detergents
Wiley, Hoboken., 18(3), 383-395.
https://doi.org/10.1007/s11743-015-1674-x

Grbavčić S, Marković D, Rajilić-Stojanović M, Antov M, Sciban M, Karadžić I, Knežević-Jugović Z. Development of an Environmentally Acceptable Detergent Formulation for Fatty Soils Based on the Lipase from the Indigenous Extremophile Pseudomonas aeruginosa Strain. in Journal of Surfactants and Detergents. 2015;18(3):383-395.
doi:10.1007/s11743-015-1674-x .

Grbavčić, Sanja, Marković, Darka, Rajilić-Stojanović, Mirjana, Antov, Mirjana, Sciban, Marina, Karadžić, Ivanka, Knežević-Jugović, Zorica, "Development of an Environmentally Acceptable Detergent Formulation for Fatty Soils Based on the Lipase from the Indigenous Extremophile Pseudomonas aeruginosa Strain" in Journal of Surfactants and Detergents, 18, no. 3 (2015):383-395,
https://doi.org/10.1007/s11743-015-1674-x . .

TY  - JOUR
AU  - Izrael Živković, Lidija T.
AU  - Živković, Ljiljana
AU  - Jokić, Bojan M.
AU  - Savić, Andrija B.
AU  - Karadžic, Ivanka M.
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5752
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.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Adsorption of Candida rugosa lipase onto alumina: effect of surface charge
EP  - 1125
IS  - 9
SP  - 1113
VL  - 80
DO  - 10.2298/JSC150222035I
ER  - 

@article{
author = "Izrael Živković, Lidija T. and Živković, Ljiljana and Jokić, Bojan M. and Savić, Andrija B. and Karadžic, 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.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Adsorption of Candida rugosa lipase onto alumina: effect of surface charge",
pages = "1125-1113",
number = "9",
volume = "80",
doi = "10.2298/JSC150222035I"
}

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

Izrael Živković LT, Živković L, Jokić BM, Savić AB, Karadžic 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., Karadžic, 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  - Zivković, Lidija T. Izrael
AU  - Živković, Ljiljana
AU  - Babić, Biljana M.
AU  - Kokunešoski, Maja
AU  - Jokić, Bojan M.
AU  - Karadzic, Ivanka M.
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5758
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.
PB  - Elsevier B.V.
T2  - Biochemical Engineering Journal
T1  - Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia
EP  - 83
SP  - 73
VL  - 93
DO  - 10.1016/j.bej.2014.09.012
ER  - 

@article{
author = "Zivković, Lidija T. Izrael 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.",
publisher = "Elsevier B.V.",
journal = "Biochemical Engineering Journal",
title = "Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia",
pages = "83-73",
volume = "93",
doi = "10.1016/j.bej.2014.09.012"
}

Zivković, L. T. I., 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
Elsevier B.V.., 93, 73-83.
https://doi.org/10.1016/j.bej.2014.09.012

Zivković LTI, 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 .

Zivković, Lidija T. Izrael, 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 . .

TY  - JOUR
AU  - Kozarski, Maja
AU  - Klaus, Anita
AU  - Jakovljević, Dragica
AU  - Todorović, Nina
AU  - Vunduk, Jovana
AU  - Petrović, Predrag
AU  - Nikšić, Miomir
AU  - Vrvić, Miroslav
AU  - van Griensven, Leo
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3051
AB  - Oxidative stress caused by an imbalanced metabolism and an excess of reactive oxygen species (ROS) lead to a range of health disorders in humans. Our endogenous antioxidant defense mechanisms and our dietary intake of antioxidants potentially regulate our oxidative homeostasis. Numerous synthetic antioxidants can effectively improve defense mechanisms, but because of their adverse toxic effects under certain conditions, preference is given to natural compounds. Consequently, the requirements for natural, alternative sources of antioxidant foods identified in edible mushrooms, as well as the mechanistic action involved in their antioxidant properties, have increased rapidly. Chemical composition and antioxidant potential of mushrooms have been intensively studied. Edible mushrooms might be used directly in enhancement of antioxidant defenses through dietary supplementation to reduce the level of oxidative stress. Wild or cultivated, they have been related to significant antioxidant properties due to their bioactive compounds, such as polyphenols, polysaccharides, vitamins, carotenoids and minerals. Antioxidant and health benefits, observed in edible mushrooms, seem an additional reason for their traditional use as a popular delicacy food. This review discusses the consumption of edible mushrooms as a powerful instrument in maintaining health, longevity and life quality.
PB  - MDPI, Basel
T2  - Molecules
T1  - Antioxidants of Edible Mushrooms
EP  - 19525
IS  - 10
SP  - 19489
VL  - 20
DO  - 10.3390/molecules201019489
ER  - 

@article{
author = "Kozarski, Maja and Klaus, Anita and Jakovljević, Dragica and Todorović, Nina and Vunduk, Jovana and Petrović, Predrag and Nikšić, Miomir and Vrvić, Miroslav and van Griensven, Leo",
year = "2015",
abstract = "Oxidative stress caused by an imbalanced metabolism and an excess of reactive oxygen species (ROS) lead to a range of health disorders in humans. Our endogenous antioxidant defense mechanisms and our dietary intake of antioxidants potentially regulate our oxidative homeostasis. Numerous synthetic antioxidants can effectively improve defense mechanisms, but because of their adverse toxic effects under certain conditions, preference is given to natural compounds. Consequently, the requirements for natural, alternative sources of antioxidant foods identified in edible mushrooms, as well as the mechanistic action involved in their antioxidant properties, have increased rapidly. Chemical composition and antioxidant potential of mushrooms have been intensively studied. Edible mushrooms might be used directly in enhancement of antioxidant defenses through dietary supplementation to reduce the level of oxidative stress. Wild or cultivated, they have been related to significant antioxidant properties due to their bioactive compounds, such as polyphenols, polysaccharides, vitamins, carotenoids and minerals. Antioxidant and health benefits, observed in edible mushrooms, seem an additional reason for their traditional use as a popular delicacy food. This review discusses the consumption of edible mushrooms as a powerful instrument in maintaining health, longevity and life quality.",
publisher = "MDPI, Basel",
journal = "Molecules",
title = "Antioxidants of Edible Mushrooms",
pages = "19525-19489",
number = "10",
volume = "20",
doi = "10.3390/molecules201019489"
}

Kozarski, M., Klaus, A., Jakovljević, D., Todorović, N., Vunduk, J., Petrović, P., Nikšić, M., Vrvić, M.,& van Griensven, L.. (2015). Antioxidants of Edible Mushrooms. in Molecules
MDPI, Basel., 20(10), 19489-19525.
https://doi.org/10.3390/molecules201019489

Kozarski M, Klaus A, Jakovljević D, Todorović N, Vunduk J, Petrović P, Nikšić M, Vrvić M, van Griensven L. Antioxidants of Edible Mushrooms. in Molecules. 2015;20(10):19489-19525.
doi:10.3390/molecules201019489 .

Kozarski, Maja, Klaus, Anita, Jakovljević, Dragica, Todorović, Nina, Vunduk, Jovana, Petrović, Predrag, Nikšić, Miomir, Vrvić, Miroslav, van Griensven, Leo, "Antioxidants of Edible Mushrooms" in Molecules, 20, no. 10 (2015):19489-19525,
https://doi.org/10.3390/molecules201019489 . .