TY  - DATA
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - https://dais.sanu.ac.rs/123456789/13156
AB  - Figure S1: Effects on the decolorization process: HRP-MAB size (a) AB225, (b) AV109; MAG-alginate ratio (c) AB225, (d) AV109; initial HRP concentration (e) AB225, (f) AV109; HRP-MAB mass (g) AB225, (h) AV109; initial H2O2 concentration (i) AB225, (j) AV109 and initial dye concentration (k) AB225, (l) AV109; Table S1: Reaction conditions for the optimization of decolorization process of AB225 and AV109 color
PB  - MDPI AG
T2  - Polymers
T1  - Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614
VL  - 14
UR  - https://hdl.handle.net/21.15107/rcub_dais_13156
ER  - 

@misc{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Đorđević, Verica and Milašinović, Nikola and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2022",
abstract = "Figure S1: Effects on the decolorization process: HRP-MAB size (a) AB225, (b) AV109; MAG-alginate ratio (c) AB225, (d) AV109; initial HRP concentration (e) AB225, (f) AV109; HRP-MAB mass (g) AB225, (h) AV109; initial H2O2 concentration (i) AB225, (j) AV109 and initial dye concentration (k) AB225, (l) AV109; Table S1: Reaction conditions for the optimization of decolorization process of AB225 and AV109 color",
publisher = "MDPI AG",
journal = "Polymers",
title = "Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614",
volume = "14",
url = "https://hdl.handle.net/21.15107/rcub_dais_13156"
}

Jonović, M., Jugović, B., Žuža, M., Đorđević, V., Milašinović, N., Bugarski, B.,& Knežević-Jugović, Z.. (2022). Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614. in Polymers
MDPI AG., 14.
https://hdl.handle.net/21.15107/rcub_dais_13156

Jonović M, Jugović B, Žuža M, Đorđević V, Milašinović N, Bugarski B, Knežević-Jugović Z. Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614. in Polymers. 2022;14.
https://hdl.handle.net/21.15107/rcub_dais_13156 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614" in Polymers, 14 (2022),
https://hdl.handle.net/21.15107/rcub_dais_13156 .

TY  - JOUR
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - https://dais.sanu.ac.rs/123456789/13155
AB  - The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.
PB  - MDPI AG
T2  - Polymers
T1  - Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation
SP  - 2614
VL  - 14
IS  - 13
DO  - 10.3390/polym14132614
UR  - https://hdl.handle.net/21.15107/rcub_dais_13155
ER  - 

@article{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Đorđević, Verica and Milašinović, Nikola and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2022",
abstract = "The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.",
publisher = "MDPI AG",
journal = "Polymers",
title = "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation",
pages = "2614",
volume = "14",
number = "13",
doi = "10.3390/polym14132614",
url = "https://hdl.handle.net/21.15107/rcub_dais_13155"
}

Jonović, M., Jugović, B., Žuža, M., Đorđević, V., Milašinović, N., Bugarski, B.,& Knežević-Jugović, Z.. (2022). Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers
MDPI AG., 14(13), 2614.
https://doi.org/10.3390/polym14132614
https://hdl.handle.net/21.15107/rcub_dais_13155

Jonović M, Jugović B, Žuža M, Đorđević V, Milašinović N, Bugarski B, Knežević-Jugović Z. Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers. 2022;14(13):2614.
doi:10.3390/polym14132614
https://hdl.handle.net/21.15107/rcub_dais_13155 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614,
https://doi.org/10.3390/polym14132614 .,
https://hdl.handle.net/21.15107/rcub_dais_13155 .

TY  - JOUR
AU  - Jonović, Marko
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Šekuljica, Nataša
AU  - Milivojević, Milan
AU  - Jugović, Branimir
AU  - Bugarski, Branko
AU  - Knežević Jugović, Zorica
PY  - 2021
UR  - https://dais.sanu.ac.rs/123456789/12087
AB  - Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 +/- 23 mu m) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 +/- 103 nm and 394 +/- 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 +/- 4 mg g(-1) on the carrier and the highest immobilized alcalase activity of 2716.1 IU g(-1) in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.
PB  - Basel : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - catalysts
T1  - Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins
SP  - 305
VL  - 11
IS  - 3
DO  - 10.3390/catal11030305
UR  - https://hdl.handle.net/21.15107/rcub_dais_12087
ER  - 

@article{
author = "Jonović, Marko and Žuža, Milena and Đorđević, Verica and Šekuljica, Nataša and Milivojević, Milan and Jugović, Branimir and Bugarski, Branko and Knežević Jugović, Zorica",
year = "2021",
abstract = "Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 +/- 23 mu m) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 +/- 103 nm and 394 +/- 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 +/- 4 mg g(-1) on the carrier and the highest immobilized alcalase activity of 2716.1 IU g(-1) in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.",
publisher = "Basel : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "catalysts",
title = "Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins",
pages = "305",
volume = "11",
number = "3",
doi = "10.3390/catal11030305",
url = "https://hdl.handle.net/21.15107/rcub_dais_12087"
}

Jonović, M., Žuža, M., Đorđević, V., Šekuljica, N., Milivojević, M., Jugović, B., Bugarski, B.,& Knežević Jugović, Z.. (2021). Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins. in catalysts
Basel : Multidisciplinary Digital Publishing Institute (MDPI)., 11(3), 305.
https://doi.org/10.3390/catal11030305
https://hdl.handle.net/21.15107/rcub_dais_12087

Jonović M, Žuža M, Đorđević V, Šekuljica N, Milivojević M, Jugović B, Bugarski B, Knežević Jugović Z. Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins. in catalysts. 2021;11(3):305.
doi:10.3390/catal11030305
https://hdl.handle.net/21.15107/rcub_dais_12087 .

Jonović, Marko, Žuža, Milena, Đorđević, Verica, Šekuljica, Nataša, Milivojević, Milan, Jugović, Branimir, Bugarski, Branko, Knežević Jugović, Zorica, "Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins" in catalysts, 11, no. 3 (2021):305,
https://doi.org/10.3390/catal11030305 .,
https://hdl.handle.net/21.15107/rcub_dais_12087 .

TY  - JOUR
AU  - Radovanović, Mirjana N.
AU  - Nikolić, Milan P.
AU  - Đurović, Vesna M.
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Grgur, Branimir
AU  - Knežević Jugović, Zorica
PY  - 2018
UR  - https://dais.sanu.ac.rs/123456789/3749
AB  - Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+ and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of α-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of α-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L–1 for MAG-A and MAG-PANI-A, respectively, while Vm was 0.19 g L–1 min–1 for MAG and 0.32 g L–1 min–1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydro-lyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hyd-rolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8±1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by α-amylase adsorbed onto MAG-PANI. © 2018, Association of Chemists and Chemical Engineers of Serbia. All rights reserved.
PB  - Belgrade : Association of Chemists and Chemical Engineers of Serbia
T2  - Hemijska industrija
T1  - Polyaniline stabilization of magnetic particles and immobilization of α-amylase
SP  - 1
EP  - 12
VL  - 72
IS  - 1
DO  - 10.2298/HEMIND161213016R
UR  - https://hdl.handle.net/21.15107/rcub_dais_3749
ER  - 

@article{
author = "Radovanović, Mirjana N. and Nikolić, Milan P. and Đurović, Vesna M. and Jugović, Branimir and Gvozdenović, Milica M. and Grgur, Branimir and Knežević Jugović, Zorica",
year = "2018",
abstract = "Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+ and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of α-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of α-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L–1 for MAG-A and MAG-PANI-A, respectively, while Vm was 0.19 g L–1 min–1 for MAG and 0.32 g L–1 min–1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydro-lyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hyd-rolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8±1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by α-amylase adsorbed onto MAG-PANI. © 2018, Association of Chemists and Chemical Engineers of Serbia. All rights reserved.",
publisher = "Belgrade : Association of Chemists and Chemical Engineers of Serbia",
journal = "Hemijska industrija",
title = "Polyaniline stabilization of magnetic particles and immobilization of α-amylase",
pages = "1-12",
volume = "72",
number = "1",
doi = "10.2298/HEMIND161213016R",
url = "https://hdl.handle.net/21.15107/rcub_dais_3749"
}

Radovanović, M. N., Nikolić, M. P., Đurović, V. M., Jugović, B., Gvozdenović, M. M., Grgur, B.,& Knežević Jugović, Z.. (2018). Polyaniline stabilization of magnetic particles and immobilization of α-amylase. in Hemijska industrija
Belgrade : Association of Chemists and Chemical Engineers of Serbia., 72(1), 1-12.
https://doi.org/10.2298/HEMIND161213016R
https://hdl.handle.net/21.15107/rcub_dais_3749

Radovanović MN, Nikolić MP, Đurović VM, Jugović B, Gvozdenović MM, Grgur B, Knežević Jugović Z. Polyaniline stabilization of magnetic particles and immobilization of α-amylase. in Hemijska industrija. 2018;72(1):1-12.
doi:10.2298/HEMIND161213016R
https://hdl.handle.net/21.15107/rcub_dais_3749 .

Radovanović, Mirjana N., Nikolić, Milan P., Đurović, Vesna M., Jugović, Branimir, Gvozdenović, Milica M., Grgur, Branimir, Knežević Jugović, Zorica, "Polyaniline stabilization of magnetic particles and immobilization of α-amylase" in Hemijska industrija, 72, no. 1 (2018):1-12,
https://doi.org/10.2298/HEMIND161213016R .,
https://hdl.handle.net/21.15107/rcub_dais_3749 .

TY  - JOUR
AU  - Jugović, Branimir
AU  - Grgur, Branimir
AU  - Antov, Mirjana
AU  - Knežević Jugović, Zorica
AU  - Stevanović, Jasmina S.
AU  - Gvozdenović, Milica M.
PY  - 2016
UR  - https://dais.sanu.ac.rs/123456789/15979
AB  - Polypyrrole enzyme electrode was formed by immobilization of glucose oxidase via glutaraldehyde into electrochemically synthesized polypyrrole on glassy carbon electrode. Electrochemical synthesis was performed in 0.5 mol dm(-3) HCl and 0.2 mol dm(-3) pyrrole at constant current density of 2 mA cm(-2). Chronopotentiometric curves of polypyrrole enzyme electrode were recorded at current density of 42 nA cm(-2) for different glucose concentrations. The determined value of the apparent Michaelis-Menten constant was 0.045 mmol dm(-3) which is significantly lower than that of free enzyme indicating enhanced enzyme efficiency when it is immobilized into electroconducting polymer matrix.
T2  - International Journal of Electrochemcal Science
T1  - Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose
SP  - 1152
EP  - 1161
VL  - 11
IS  - 2
UR  - https://hdl.handle.net/21.15107/rcub_dais_15979
ER  - 

@article{
author = "Jugović, Branimir and Grgur, Branimir and Antov, Mirjana and Knežević Jugović, Zorica and Stevanović, Jasmina S. and Gvozdenović, Milica M.",
year = "2016",
abstract = "Polypyrrole enzyme electrode was formed by immobilization of glucose oxidase via glutaraldehyde into electrochemically synthesized polypyrrole on glassy carbon electrode. Electrochemical synthesis was performed in 0.5 mol dm(-3) HCl and 0.2 mol dm(-3) pyrrole at constant current density of 2 mA cm(-2). Chronopotentiometric curves of polypyrrole enzyme electrode were recorded at current density of 42 nA cm(-2) for different glucose concentrations. The determined value of the apparent Michaelis-Menten constant was 0.045 mmol dm(-3) which is significantly lower than that of free enzyme indicating enhanced enzyme efficiency when it is immobilized into electroconducting polymer matrix.",
journal = "International Journal of Electrochemcal Science",
title = "Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose",
pages = "1152-1161",
volume = "11",
number = "2",
url = "https://hdl.handle.net/21.15107/rcub_dais_15979"
}

Jugović, B., Grgur, B., Antov, M., Knežević Jugović, Z., Stevanović, J. S.,& Gvozdenović, M. M.. (2016). Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose. in International Journal of Electrochemcal Science, 11(2), 1152-1161.
https://hdl.handle.net/21.15107/rcub_dais_15979

Jugović B, Grgur B, Antov M, Knežević Jugović Z, Stevanović JS, Gvozdenović MM. Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose. in International Journal of Electrochemcal Science. 2016;11(2):1152-1161.
https://hdl.handle.net/21.15107/rcub_dais_15979 .

Jugović, Branimir, Grgur, Branimir, Antov, Mirjana, Knežević Jugović, Zorica, Stevanović, Jasmina S., Gvozdenović, Milica M., "Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose" in International Journal of Electrochemcal Science, 11, no. 2 (2016):1152-1161,
https://hdl.handle.net/21.15107/rcub_dais_15979 .

TY  - JOUR
AU  - Radovanović, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Jokić, Bojan
AU  - Grgur, Branimir
AU  - Bugarski, Branko
AU  - Knežević Jugović, Zorica
PY  - 2016
UR  - https://dais.sanu.ac.rs/123456789/16002
AB  - The immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline was studied. The support was characterized by field emission scanning electron microscopy (FESEM). The obtained magnetic particles were agglomerates of nanoparticles with sizes below 100 nm. The effects of various factors on immobilization, including time, the initial enzyme concentration, pH, and temperature, were examined. The optimum pH, temperature, and time for immobilization were established to be 7, 45°C and 75 min, respectively. The maximum amount of adsorbed α-amylase of 10/100 mg support was determined at the 5 mg/mL enzyme concentration. It appeared that α-amylase was stabilized in terms of pH and temperature by adsorption on magnetic particles coated with polyaniline. The good agreement of the equilibrium data with the Langmuir isotherm model confirmed the monolayer coverage of enzyme molecules on the surface of magnetic particles, and the maximum adsorption capacity was found to be 55.6/100 mg support at 25°C. The biocatalyst retained 55.5 ± 1.63% of its initial activity after nine cycles of reuse in starch hydrolysis at 60°C in a batch reactor. The immobilized enzyme also showed very good storage stability.
PB  - Hoboken, NJ : John Wiley & Sons
T2  - Starch
T1  - Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline
SP  - 427
EP  - 435
VL  - 68
IS  - 5-6
DO  - 10.1002/star.201500161
UR  - https://hdl.handle.net/21.15107/rcub_dais_16002
ER  - 

@article{
author = "Radovanović, Mirjana and Jugović, Branimir and Gvozdenović, Milica M. and Jokić, Bojan and Grgur, Branimir and Bugarski, Branko and Knežević Jugović, Zorica",
year = "2016",
abstract = "The immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline was studied. The support was characterized by field emission scanning electron microscopy (FESEM). The obtained magnetic particles were agglomerates of nanoparticles with sizes below 100 nm. The effects of various factors on immobilization, including time, the initial enzyme concentration, pH, and temperature, were examined. The optimum pH, temperature, and time for immobilization were established to be 7, 45°C and 75 min, respectively. The maximum amount of adsorbed α-amylase of 10/100 mg support was determined at the 5 mg/mL enzyme concentration. It appeared that α-amylase was stabilized in terms of pH and temperature by adsorption on magnetic particles coated with polyaniline. The good agreement of the equilibrium data with the Langmuir isotherm model confirmed the monolayer coverage of enzyme molecules on the surface of magnetic particles, and the maximum adsorption capacity was found to be 55.6/100 mg support at 25°C. The biocatalyst retained 55.5 ± 1.63% of its initial activity after nine cycles of reuse in starch hydrolysis at 60°C in a batch reactor. The immobilized enzyme also showed very good storage stability.",
publisher = "Hoboken, NJ : John Wiley & Sons",
journal = "Starch",
title = "Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline",
pages = "427-435",
volume = "68",
number = "5-6",
doi = "10.1002/star.201500161",
url = "https://hdl.handle.net/21.15107/rcub_dais_16002"
}

Radovanović, M., Jugović, B., Gvozdenović, M. M., Jokić, B., Grgur, B., Bugarski, B.,& Knežević Jugović, Z.. (2016). Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline. in Starch
Hoboken, NJ : John Wiley & Sons., 68(5-6), 427-435.
https://doi.org/10.1002/star.201500161
https://hdl.handle.net/21.15107/rcub_dais_16002

Radovanović M, Jugović B, Gvozdenović MM, Jokić B, Grgur B, Bugarski B, Knežević Jugović Z. Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline. in Starch. 2016;68(5-6):427-435.
doi:10.1002/star.201500161
https://hdl.handle.net/21.15107/rcub_dais_16002 .

Radovanović, Mirjana, Jugović, Branimir, Gvozdenović, Milica M., Jokić, Bojan, Grgur, Branimir, Bugarski, Branko, Knežević Jugović, Zorica, "Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline" in Starch, 68, no. 5-6 (2016):427-435,
https://doi.org/10.1002/star.201500161 .,
https://hdl.handle.net/21.15107/rcub_dais_16002 .

TY  - JOUR
AU  - Šekuljica, Nataša Ž.
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
AU  - Jugović, Branimir
AU  - Grgur, Branimir
PY  - 2016
UR  - https://dais.sanu.ac.rs/123456789/16004
AB  - The potential application of electrochemically formed copper sulfide as horseradish peroxidase mediator in the enzymatic biofuel cell and anthraquinone AV109 dye as a fuel is investigated. The open circuit voltage of 0.52 V and short circuit current of ∼3.6 µA/cm2 are obtained, with the maximum specific power of ∼1 µW/cm2. The influence of internal resistance of the cell is discussed. Decolorization is investigated under open circuit potentials, and under external load of 3.3 kΩ conditions. In both cases, 40% of decolorization is achieved, but are three times faster under external load conditions. Specific energy during decolorization in such cell is estimated to ∼5 mWh/m2. The possible mechanism of the power generation during decolorization of AV 109 dye is discussed.
PB  - Elsevier
T2  - Journal of Energy Chemistry
T1  - Biofuel cell based on horseradish peroxidase immobilized on copper sulfide as anode for decolorization of anthraquinone AV109 dye
SP  - 403
EP  - 408
VL  - 25
IS  - 3
DO  - 10.1016/j.jechem.2016.03.011
UR  - https://hdl.handle.net/21.15107/rcub_dais_16004
ER  - 

@article{
author = "Šekuljica, Nataša Ž. and Gvozdenović, Milica M. and Knežević Jugović, Zorica and Jugović, Branimir and Grgur, Branimir",
year = "2016",
abstract = "The potential application of electrochemically formed copper sulfide as horseradish peroxidase mediator in the enzymatic biofuel cell and anthraquinone AV109 dye as a fuel is investigated. The open circuit voltage of 0.52 V and short circuit current of ∼3.6 µA/cm2 are obtained, with the maximum specific power of ∼1 µW/cm2. The influence of internal resistance of the cell is discussed. Decolorization is investigated under open circuit potentials, and under external load of 3.3 kΩ conditions. In both cases, 40% of decolorization is achieved, but are three times faster under external load conditions. Specific energy during decolorization in such cell is estimated to ∼5 mWh/m2. The possible mechanism of the power generation during decolorization of AV 109 dye is discussed.",
publisher = "Elsevier",
journal = "Journal of Energy Chemistry",
title = "Biofuel cell based on horseradish peroxidase immobilized on copper sulfide as anode for decolorization of anthraquinone AV109 dye",
pages = "403-408",
volume = "25",
number = "3",
doi = "10.1016/j.jechem.2016.03.011",
url = "https://hdl.handle.net/21.15107/rcub_dais_16004"
}

Šekuljica, N. Ž., Gvozdenović, M. M., Knežević Jugović, Z., Jugović, B.,& Grgur, B.. (2016). Biofuel cell based on horseradish peroxidase immobilized on copper sulfide as anode for decolorization of anthraquinone AV109 dye. in Journal of Energy Chemistry
Elsevier., 25(3), 403-408.
https://doi.org/10.1016/j.jechem.2016.03.011
https://hdl.handle.net/21.15107/rcub_dais_16004

Šekuljica NŽ, Gvozdenović MM, Knežević Jugović Z, Jugović B, Grgur B. Biofuel cell based on horseradish peroxidase immobilized on copper sulfide as anode for decolorization of anthraquinone AV109 dye. in Journal of Energy Chemistry. 2016;25(3):403-408.
doi:10.1016/j.jechem.2016.03.011
https://hdl.handle.net/21.15107/rcub_dais_16004 .

Šekuljica, Nataša Ž., Gvozdenović, Milica M., Knežević Jugović, Zorica, Jugović, Branimir, Grgur, Branimir, "Biofuel cell based on horseradish peroxidase immobilized on copper sulfide as anode for decolorization of anthraquinone AV109 dye" in Journal of Energy Chemistry, 25, no. 3 (2016):403-408,
https://doi.org/10.1016/j.jechem.2016.03.011 .,
https://hdl.handle.net/21.15107/rcub_dais_16004 .

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Luković, Nevena
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Grbavčić, Sanja
AU  - Jovanović, Jelena
AU  - Knežević Jugović, Zorica
PY  - 2015
UR  - https://dais.sanu.ac.rs/123456789/3528
AB  - The objective of this research was to design an efficient continuously operated membrane reactor with a separation unit for egg white protein (EWP) hydrolysis and production of hydrolysates with improved antioxidant properties. For this purpose, a mechanically stirred tank reactor coupled with the polyethersulfone ultrafiltration module with a molecular weight cutoff of 10 kDa was employed. Several proteolytic enzymes have been tested in order to obtain the best quality of peptide-based formulations intended for human consumption. Among protease from Bacillus licheniformis (Alcalase), protease from Bacillus amyloliquefaciens (Neutrase), and protease from papaya latex (papain), the highest degree of hydrolysis (DH), as well as the best antioxidant properties of obtained hydrolysates, was achieved with Alcalase. The effects of operating variables such as enzyme/substrate ([E]/[S]) ratio, impeller speed, and permeate flow rate were further studied using response surface methodology (RSM) and Box–Behnken experimental design. Results obtained in RSM analysis confirmed that over the studied range [E]/[S] ratio, impeller speed and permeate flow rate had the significant effect on the DH and reactor capacity. The effects of different impeller geometries were also studied and four-bladed propeller stirrer enabled the highest DH. Antioxidant properties were analyzed by the 2,2-diphenyl-1-picrylhydrazyl (DPPH), by the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, and by the linear voltammetry methods. Results show that the use of Alcalase in the membrane reactor system is of potential interest for the EWP hydrolysis and obtaining value-added egg products. © 2014, Springer Science+Business Media New York.
PB  - Springer
T2  - Food and Bioprocess Technology
T1  - Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit
SP  - 287
EP  - 300
VL  - 8
IS  - 2
DO  - 10.1007/s11947-014-1402-y
UR  - https://hdl.handle.net/21.15107/rcub_dais_3528
ER  - 

@article{
author = "Jakovetić, Sonja and Luković, Nevena and Jugović, Branimir and Gvozdenović, Milica M. and Grbavčić, Sanja and Jovanović, Jelena and Knežević Jugović, Zorica",
year = "2015",
abstract = "The objective of this research was to design an efficient continuously operated membrane reactor with a separation unit for egg white protein (EWP) hydrolysis and production of hydrolysates with improved antioxidant properties. For this purpose, a mechanically stirred tank reactor coupled with the polyethersulfone ultrafiltration module with a molecular weight cutoff of 10 kDa was employed. Several proteolytic enzymes have been tested in order to obtain the best quality of peptide-based formulations intended for human consumption. Among protease from Bacillus licheniformis (Alcalase), protease from Bacillus amyloliquefaciens (Neutrase), and protease from papaya latex (papain), the highest degree of hydrolysis (DH), as well as the best antioxidant properties of obtained hydrolysates, was achieved with Alcalase. The effects of operating variables such as enzyme/substrate ([E]/[S]) ratio, impeller speed, and permeate flow rate were further studied using response surface methodology (RSM) and Box–Behnken experimental design. Results obtained in RSM analysis confirmed that over the studied range [E]/[S] ratio, impeller speed and permeate flow rate had the significant effect on the DH and reactor capacity. The effects of different impeller geometries were also studied and four-bladed propeller stirrer enabled the highest DH. Antioxidant properties were analyzed by the 2,2-diphenyl-1-picrylhydrazyl (DPPH), by the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, and by the linear voltammetry methods. Results show that the use of Alcalase in the membrane reactor system is of potential interest for the EWP hydrolysis and obtaining value-added egg products. © 2014, Springer Science+Business Media New York.",
publisher = "Springer",
journal = "Food and Bioprocess Technology",
title = "Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit",
pages = "287-300",
volume = "8",
number = "2",
doi = "10.1007/s11947-014-1402-y",
url = "https://hdl.handle.net/21.15107/rcub_dais_3528"
}

Jakovetić, S., Luković, N., Jugović, B., Gvozdenović, M. M., Grbavčić, S., Jovanović, J.,& Knežević Jugović, Z.. (2015). Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit. in Food and Bioprocess Technology
Springer., 8(2), 287-300.
https://doi.org/10.1007/s11947-014-1402-y
https://hdl.handle.net/21.15107/rcub_dais_3528

Jakovetić S, Luković N, Jugović B, Gvozdenović MM, Grbavčić S, Jovanović J, Knežević Jugović Z. Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit. in Food and Bioprocess Technology. 2015;8(2):287-300.
doi:10.1007/s11947-014-1402-y
https://hdl.handle.net/21.15107/rcub_dais_3528 .

Jakovetić, Sonja, Luković, Nevena, Jugović, Branimir, Gvozdenović, Milica M., Grbavčić, Sanja, Jovanović, Jelena, Knežević Jugović, Zorica, "Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit" in Food and Bioprocess Technology, 8, no. 2 (2015):287-300,
https://doi.org/10.1007/s11947-014-1402-y .,
https://hdl.handle.net/21.15107/rcub_dais_3528 .

TY  - JOUR
AU  - Popović, Nataša
AU  - Jugović, Branimir
AU  - Jokić, Bojan
AU  - Knežević Jugović, Zorica
AU  - Stevanović, Jasmina S.
AU  - Grgur, Branimir
AU  - Gvozdenović, Milica M.
PY  - 2015
UR  - https://dais.sanu.ac.rs/123456789/3543
UR  - http://www.electrochemsci.org/papers/vol10/100201208.pdf
AB  - Electrochemical formation of polyaniline (PANI) modified electrode was performed galvanostatically from aqueous solution of 1.0 mol dm-3 HCl containing 0.2 mol dm-3 aniline at current densities ranging from 0.5-3.0 mA cm-2. The morphology of PANI electrode consisted of highly developed nanofibrous network with electrocatalytic features towards oxidation of ascorbic acid, reflected in increase of the peak current ~ 2.5 times and shift of the oxidation potential by 0.32 V to less positive values. Response of PANI modified electrode was obtained from anodic LSV curves. Current peak potentials decreased with increase of pH with slope of ~ 32 mV pH-1, indicating two electron charge transfer process with liberation of one proton characteristic of an electrochemical reaction followed by a chemical step. © 2015 The Authors.
PB  - Belgrade : ESG
T2  - International Journal of Electrochemical Science
T1  - Electrochemical template-free synthesis of nanofibrous polyaniline modified electrode for ascorbic acid determination
SP  - 1208
EP  - 1220
VL  - 10
IS  - 2
UR  - https://hdl.handle.net/21.15107/rcub_dais_3543
ER  - 

@article{
author = "Popović, Nataša and Jugović, Branimir and Jokić, Bojan and Knežević Jugović, Zorica and Stevanović, Jasmina S. and Grgur, Branimir and Gvozdenović, Milica M.",
year = "2015",
abstract = "Electrochemical formation of polyaniline (PANI) modified electrode was performed galvanostatically from aqueous solution of 1.0 mol dm-3 HCl containing 0.2 mol dm-3 aniline at current densities ranging from 0.5-3.0 mA cm-2. The morphology of PANI electrode consisted of highly developed nanofibrous network with electrocatalytic features towards oxidation of ascorbic acid, reflected in increase of the peak current ~ 2.5 times and shift of the oxidation potential by 0.32 V to less positive values. Response of PANI modified electrode was obtained from anodic LSV curves. Current peak potentials decreased with increase of pH with slope of ~ 32 mV pH-1, indicating two electron charge transfer process with liberation of one proton characteristic of an electrochemical reaction followed by a chemical step. © 2015 The Authors.",
publisher = "Belgrade : ESG",
journal = "International Journal of Electrochemical Science",
title = "Electrochemical template-free synthesis of nanofibrous polyaniline modified electrode for ascorbic acid determination",
pages = "1208-1220",
volume = "10",
number = "2",
url = "https://hdl.handle.net/21.15107/rcub_dais_3543"
}

Popović, N., Jugović, B., Jokić, B., Knežević Jugović, Z., Stevanović, J. S., Grgur, B.,& Gvozdenović, M. M.. (2015). Electrochemical template-free synthesis of nanofibrous polyaniline modified electrode for ascorbic acid determination. in International Journal of Electrochemical Science
Belgrade : ESG., 10(2), 1208-1220.
https://hdl.handle.net/21.15107/rcub_dais_3543

Popović N, Jugović B, Jokić B, Knežević Jugović Z, Stevanović JS, Grgur B, Gvozdenović MM. Electrochemical template-free synthesis of nanofibrous polyaniline modified electrode for ascorbic acid determination. in International Journal of Electrochemical Science. 2015;10(2):1208-1220.
https://hdl.handle.net/21.15107/rcub_dais_3543 .

Popović, Nataša, Jugović, Branimir, Jokić, Bojan, Knežević Jugović, Zorica, Stevanović, Jasmina S., Grgur, Branimir, Gvozdenović, Milica M., "Electrochemical template-free synthesis of nanofibrous polyaniline modified electrode for ascorbic acid determination" in International Journal of Electrochemical Science, 10, no. 2 (2015):1208-1220,
https://hdl.handle.net/21.15107/rcub_dais_3543 .

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Mijin, Dušan
AU  - Knežević Jugović, Zorica
PY  - 2013
UR  - https://dais.sanu.ac.rs/123456789/355
AB  - Immobilized lipase from Candida antarctica (Novozyme 435) was tested for the synthesis of various phenolic acid esters (ethyl and n-butyl cinnamate, ethyl p-coumarate and n-butyl p-methoxycinnamate). The second-order kinetic model was used to mathematically describe the reaction kinetics and to compare present processes quantitatively. It was found that the model agreed well with the experimental data. Further, the effect of alcohol type on the esterification of cinnamic acid was investigated. The immobilized lipase showed more ability to catalyze the synthesis of butyl cinnamate. Therefore, the process was optimized for the synthesis of butyl cinnamate as a function of solvent polarity (logP) and amount of biocatalyst. The highest ester yield of 60.7 % was obtained for the highest enzyme concentration tested (3 % w/w), but the productivity was for 34 % lower than the corresponding value obtained for the enzyme concentration of 1 % (w/w). The synthesized esters were purified, identified, and screened for antioxidant activities. Both DPPH assay and cyclic voltammetry measurement have shown that cinnamic acid esters have better antioxidant properties than cinnamic acid itself.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica
SP  - 1560
EP  - 1573
VL  - 170
IS  - 7
DO  - 10.1007/s12010-013-0294-z
UR  - https://hdl.handle.net/21.15107/rcub_dais_355
ER  - 

@article{
author = "Jakovetić, Sonja and Jugović, Branimir and Gvozdenović, Milica M. and Bezbradica, Dejan and Antov, Mirjana and Mijin, Dušan and Knežević Jugović, Zorica",
year = "2013",
abstract = "Immobilized lipase from Candida antarctica (Novozyme 435) was tested for the synthesis of various phenolic acid esters (ethyl and n-butyl cinnamate, ethyl p-coumarate and n-butyl p-methoxycinnamate). The second-order kinetic model was used to mathematically describe the reaction kinetics and to compare present processes quantitatively. It was found that the model agreed well with the experimental data. Further, the effect of alcohol type on the esterification of cinnamic acid was investigated. The immobilized lipase showed more ability to catalyze the synthesis of butyl cinnamate. Therefore, the process was optimized for the synthesis of butyl cinnamate as a function of solvent polarity (logP) and amount of biocatalyst. The highest ester yield of 60.7 % was obtained for the highest enzyme concentration tested (3 % w/w), but the productivity was for 34 % lower than the corresponding value obtained for the enzyme concentration of 1 % (w/w). The synthesized esters were purified, identified, and screened for antioxidant activities. Both DPPH assay and cyclic voltammetry measurement have shown that cinnamic acid esters have better antioxidant properties than cinnamic acid itself.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica",
pages = "1560-1573",
volume = "170",
number = "7",
doi = "10.1007/s12010-013-0294-z",
url = "https://hdl.handle.net/21.15107/rcub_dais_355"
}

Jakovetić, S., Jugović, B., Gvozdenović, M. M., Bezbradica, D., Antov, M., Mijin, D.,& Knežević Jugović, Z.. (2013). Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica. in Applied Biochemistry and Biotechnology
Springer., 170(7), 1560-1573.
https://doi.org/10.1007/s12010-013-0294-z
https://hdl.handle.net/21.15107/rcub_dais_355

Jakovetić S, Jugović B, Gvozdenović MM, Bezbradica D, Antov M, Mijin D, Knežević Jugović Z. Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica. in Applied Biochemistry and Biotechnology. 2013;170(7):1560-1573.
doi:10.1007/s12010-013-0294-z
https://hdl.handle.net/21.15107/rcub_dais_355 .

Jakovetić, Sonja, Jugović, Branimir, Gvozdenović, Milica M., Bezbradica, Dejan, Antov, Mirjana, Mijin, Dušan, Knežević Jugović, Zorica, "Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica" in Applied Biochemistry and Biotechnology, 170, no. 7 (2013):1560-1573,
https://doi.org/10.1007/s12010-013-0294-z .,
https://hdl.handle.net/21.15107/rcub_dais_355 .

TY  - CONF
AU  - Knežević Jugović, Zorica
AU  - Gluvić, Ana
AU  - Žuža, Milena
AU  - Stefanović, Andrea
AU  - Gvozdenović, Milica M.
AU  - Jugović, Branimir
AU  - Antov, Mirjana
PY  - 2013
UR  - https://dais.sanu.ac.rs/123456789/387
AB  - Enzymatic hydrolysis of egg white proteins has shown great potential to improve their functional properties such as increased solubility, stability, and digestibility, and to reduce protein allergenicity while still retaining their nutrition value. However, the enzymatic hydrolysis process is still poorly defined and difficult to control at the industrial scale resulting in peptide
mixtures poorly characterized and with unpleasant bitter taste that make them unsuitable for human consumption. Thus, the hydrolysis reaction must be carefully controlled in order to produce new value-added egg white hydrolysates with improved properties and specialized functionality. In this paper egg white protein solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis. The hydrolysate was then tested on antioxidant
activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. All
protein hydrolysates showed higher solubility and digestibility than intact proteins, especially at
pHs near isoelectric point of egg white proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the native protein solution.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering
T1  - Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates
SP  - 1433
EP  - 1439
UR  - https://hdl.handle.net/21.15107/rcub_dais_387
ER  - 

@conference{
author = "Knežević Jugović, Zorica and Gluvić, Ana and Žuža, Milena and Stefanović, Andrea and Gvozdenović, Milica M. and Jugović, Branimir and Antov, Mirjana",
year = "2013",
abstract = "Enzymatic hydrolysis of egg white proteins has shown great potential to improve their functional properties such as increased solubility, stability, and digestibility, and to reduce protein allergenicity while still retaining their nutrition value. However, the enzymatic hydrolysis process is still poorly defined and difficult to control at the industrial scale resulting in peptide
mixtures poorly characterized and with unpleasant bitter taste that make them unsuitable for human consumption. Thus, the hydrolysis reaction must be carefully controlled in order to produce new value-added egg white hydrolysates with improved properties and specialized functionality. In this paper egg white protein solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis. The hydrolysate was then tested on antioxidant
activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. All
protein hydrolysates showed higher solubility and digestibility than intact proteins, especially at
pHs near isoelectric point of egg white proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the native protein solution.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering",
title = "Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates",
pages = "1433-1439",
url = "https://hdl.handle.net/21.15107/rcub_dais_387"
}

Knežević Jugović, Z., Gluvić, A., Žuža, M., Stefanović, A., Gvozdenović, M. M., Jugović, B.,& Antov, M.. (2013). Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates. in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1433-1439.
https://hdl.handle.net/21.15107/rcub_dais_387

Knežević Jugović Z, Gluvić A, Žuža M, Stefanović A, Gvozdenović MM, Jugović B, Antov M. Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates. in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering. 2013;:1433-1439.
https://hdl.handle.net/21.15107/rcub_dais_387 .

Knežević Jugović, Zorica, Gluvić, Ana, Žuža, Milena, Stefanović, Andrea, Gvozdenović, Milica M., Jugović, Branimir, Antov, Mirjana, "Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates" in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering (2013):1433-1439,
https://hdl.handle.net/21.15107/rcub_dais_387 .

TY  - CONF
AU  - Knežević Jugović, Zorica
AU  - Jakovetić, Sonja
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Grbavčić, Sanja
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
PY  - 2012
UR  - https://dais.sanu.ac.rs/123456789/493
AB  - The esterification activity of the commercial immobilized lipase CALB towards cinnamic acids and its derivative has been studied. Using cinnamic acid as substrate, the reaction rate constants (1.95 h-1 mM-1 for ethanol and 3.07 h-1 mM-1 for butanol) were more than four and nine times higher compared to those obtained with p-coumaric (0.47 h-1 mM-1) and p-methoxycinnamic acids (0.32 h-1 mM-1), respectively. Thus, esterification of cinnamic acid with ethanol by using C. antarctica lipase has selected as a model reaction for further study. Isooctane is shown to be the best solvent for this reaction even though solubility of cinnamic acid in this a polar solvent is very low. Highest esterification yield of ethyl cinnamate is obtained when initial molar ratio of substrates 1:3 (cinnamic acid is limiting substrate) is used. Esterification of cinnamic acid appeared to result in increasing radical-scavenging ability. The effect of esterification of cinnamic acid was also confirmed by electrochemical method using ethyl cinnamate which appeared to enhance the antioxidant activity. These findings should stimulate the application of such lipase-catalyzed reactions for the preparation of food acceptable esters of cinnamic acid as potential lipophilic antioxidants.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering
T1  - Enzymatic Synthesis of Aliphatic Esters of Phenolic Acids and Evaluation of Their Antioxidant Properties
SP  - 1426
EP  - 1432
UR  - https://hdl.handle.net/21.15107/rcub_dais_493
ER  - 

@conference{
author = "Knežević Jugović, Zorica and Jakovetić, Sonja and Jugović, Branimir and Gvozdenović, Milica M. and Grbavčić, Sanja and Bezbradica, Dejan and Antov, Mirjana",
year = "2012",
abstract = "The esterification activity of the commercial immobilized lipase CALB towards cinnamic acids and its derivative has been studied. Using cinnamic acid as substrate, the reaction rate constants (1.95 h-1 mM-1 for ethanol and 3.07 h-1 mM-1 for butanol) were more than four and nine times higher compared to those obtained with p-coumaric (0.47 h-1 mM-1) and p-methoxycinnamic acids (0.32 h-1 mM-1), respectively. Thus, esterification of cinnamic acid with ethanol by using C. antarctica lipase has selected as a model reaction for further study. Isooctane is shown to be the best solvent for this reaction even though solubility of cinnamic acid in this a polar solvent is very low. Highest esterification yield of ethyl cinnamate is obtained when initial molar ratio of substrates 1:3 (cinnamic acid is limiting substrate) is used. Esterification of cinnamic acid appeared to result in increasing radical-scavenging ability. The effect of esterification of cinnamic acid was also confirmed by electrochemical method using ethyl cinnamate which appeared to enhance the antioxidant activity. These findings should stimulate the application of such lipase-catalyzed reactions for the preparation of food acceptable esters of cinnamic acid as potential lipophilic antioxidants.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering",
title = "Enzymatic Synthesis of Aliphatic Esters of Phenolic Acids and Evaluation of Their Antioxidant Properties",
pages = "1426-1432",
url = "https://hdl.handle.net/21.15107/rcub_dais_493"
}

Knežević Jugović, Z., Jakovetić, S., Jugović, B., Gvozdenović, M. M., Grbavčić, S., Bezbradica, D.,& Antov, M.. (2012). Enzymatic Synthesis of Aliphatic Esters of Phenolic Acids and Evaluation of Their Antioxidant Properties. in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1426-1432.
https://hdl.handle.net/21.15107/rcub_dais_493

Knežević Jugović Z, Jakovetić S, Jugović B, Gvozdenović MM, Grbavčić S, Bezbradica D, Antov M. Enzymatic Synthesis of Aliphatic Esters of Phenolic Acids and Evaluation of Their Antioxidant Properties. in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering. 2012;:1426-1432.
https://hdl.handle.net/21.15107/rcub_dais_493 .

Knežević Jugović, Zorica, Jakovetić, Sonja, Jugović, Branimir, Gvozdenović, Milica M., Grbavčić, Sanja, Bezbradica, Dejan, Antov, Mirjana, "Enzymatic Synthesis of Aliphatic Esters of Phenolic Acids and Evaluation of Their Antioxidant Properties" in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering (2012):1426-1432,
https://hdl.handle.net/21.15107/rcub_dais_493 .

TY  - JOUR
AU  - Antov, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
PY  - 2012
UR  - https://dais.sanu.ac.rs/123456789/459
AB  - This study is concerned with the partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. In the system of 10% (w/w) polyethylene glycol 1500/5% (w/w) dextran 500,000/80% (w/w) crude enzyme at the pH 5, 100%, yield of cellulolytic activity from Penicillium sp. in the top phase was achieved in a single extraction step. Addition of KH2PO4 to this system at a concentration of 15 mmol/L improved the purification factor in the top phase for cellulolytic activity from crude preparation to a value of 2.6, although it had an adverse effect on the yield in the same phase. [Projekat Ministarstva nauke Republike Srbije, br. 46010]
PB  - Belgrade : Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems
SP  - 151
EP  - 158
DO  - 10.2298/APT1243151A
UR  - https://hdl.handle.net/21.15107/rcub_dais_459
ER  - 

@article{
author = "Antov, Mirjana and Jugović, Branimir and Gvozdenović, Milica M. and Knežević Jugović, Zorica",
year = "2012",
abstract = "This study is concerned with the partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. In the system of 10% (w/w) polyethylene glycol 1500/5% (w/w) dextran 500,000/80% (w/w) crude enzyme at the pH 5, 100%, yield of cellulolytic activity from Penicillium sp. in the top phase was achieved in a single extraction step. Addition of KH2PO4 to this system at a concentration of 15 mmol/L improved the purification factor in the top phase for cellulolytic activity from crude preparation to a value of 2.6, although it had an adverse effect on the yield in the same phase. [Projekat Ministarstva nauke Republike Srbije, br. 46010]",
publisher = "Belgrade : Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems",
pages = "151-158",
doi = "10.2298/APT1243151A",
url = "https://hdl.handle.net/21.15107/rcub_dais_459"
}

Antov, M., Jugović, B., Gvozdenović, M. M.,& Knežević Jugović, Z.. (2012). Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. in Acta periodica technologica
Belgrade : Faculty of Technology, Novi Sad., 151-158.
https://doi.org/10.2298/APT1243151A
https://hdl.handle.net/21.15107/rcub_dais_459

Antov M, Jugović B, Gvozdenović MM, Knežević Jugović Z. Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. in Acta periodica technologica. 2012;:151-158.
doi:10.2298/APT1243151A
https://hdl.handle.net/21.15107/rcub_dais_459 .

Antov, Mirjana, Jugović, Branimir, Gvozdenović, Milica M., Knežević Jugović, Zorica, "Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems" in Acta periodica technologica (2012):151-158,
https://doi.org/10.2298/APT1243151A .,
https://hdl.handle.net/21.15107/rcub_dais_459 .

TY  - CONF
AU  - Antov, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
PY  - 2012
UR  - https://dais.sanu.ac.rs/123456789/448
AB  - Aqueous two-phase systems can be formed by mixing the solutions of two mutually incompatible polymers or polymer and salt above critical concentrations and represent media that are very well suited for the separation and purification of biomolecules. The basis of separation is uneven distribution of biomolecules between two phases both having high water content. This so-called biocompatibility of phases allows preservation of biomolecules’ native structure while the presence of polymer can even improve their stability. Partitioning is governed by numerous factors that can be manipulated to achieve desired separation and purification results, which makes aqueous two-phase system very flexible for application.
Cellulases, enzymes belonging to family of glycosyl hydrolases, play key role in organic carbon turnover and have important and wide application in industry. Extraction of enzymes in aqueous two-phase systems has been recognized as useful technique in downstream processing for their isolation and purification. In this study, partitioning of cellulases in
polyethylene glycol/dextran and polyethylene glycol/salt two-phase systems was investigated with the aim to determine the most appropriate molecular weight of polymers, kind of salt and concentration of aqueous two-phase constituents at
which the highest possible yield and purification factor in the top phase can be achieved.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering
T1  - Partitioning and purification of cellulases in aqueous two-phase system
SP  - 1346
EP  - 1346
UR  - https://hdl.handle.net/21.15107/rcub_dais_448
ER  - 

@conference{
author = "Antov, Mirjana and Jugović, Branimir and Gvozdenović, Milica M. and Knežević Jugović, Zorica",
year = "2012",
abstract = "Aqueous two-phase systems can be formed by mixing the solutions of two mutually incompatible polymers or polymer and salt above critical concentrations and represent media that are very well suited for the separation and purification of biomolecules. The basis of separation is uneven distribution of biomolecules between two phases both having high water content. This so-called biocompatibility of phases allows preservation of biomolecules’ native structure while the presence of polymer can even improve their stability. Partitioning is governed by numerous factors that can be manipulated to achieve desired separation and purification results, which makes aqueous two-phase system very flexible for application.
Cellulases, enzymes belonging to family of glycosyl hydrolases, play key role in organic carbon turnover and have important and wide application in industry. Extraction of enzymes in aqueous two-phase systems has been recognized as useful technique in downstream processing for their isolation and purification. In this study, partitioning of cellulases in
polyethylene glycol/dextran and polyethylene glycol/salt two-phase systems was investigated with the aim to determine the most appropriate molecular weight of polymers, kind of salt and concentration of aqueous two-phase constituents at
which the highest possible yield and purification factor in the top phase can be achieved.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering",
title = "Partitioning and purification of cellulases in aqueous two-phase system",
pages = "1346-1346",
url = "https://hdl.handle.net/21.15107/rcub_dais_448"
}

Antov, M., Jugović, B., Gvozdenović, M. M.,& Knežević Jugović, Z.. (2012). Partitioning and purification of cellulases in aqueous two-phase system. in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1346-1346.
https://hdl.handle.net/21.15107/rcub_dais_448

Antov M, Jugović B, Gvozdenović MM, Knežević Jugović Z. Partitioning and purification of cellulases in aqueous two-phase system. in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering. 2012;:1346-1346.
https://hdl.handle.net/21.15107/rcub_dais_448 .

Antov, Mirjana, Jugović, Branimir, Gvozdenović, Milica M., Knežević Jugović, Zorica, "Partitioning and purification of cellulases in aqueous two-phase system" in Proceedings of the 39th International Conference of Slovak Society of Chemical Engineering (2012):1346-1346,
https://hdl.handle.net/21.15107/rcub_dais_448 .

TY  - CONF
AU  - Antov, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
PY  - 2012
UR  - https://dais.sanu.ac.rs/123456789/139
AB  - Poster presented at the 39th International Conference of Slovak Society of Chemical Engineering, Tatranske Matliare, Slovakia, May 21–25, 2012
T1  - Partitioning and purification of cellulases in aqueous two-phase system
UR  - https://hdl.handle.net/21.15107/rcub_dais_139
ER  - 

@conference{
author = "Antov, Mirjana and Jugović, Branimir and Gvozdenović, Milica M. and Knežević Jugović, Zorica",
year = "2012",
abstract = "Poster presented at the 39th International Conference of Slovak Society of Chemical Engineering, Tatranske Matliare, Slovakia, May 21–25, 2012",
title = "Partitioning and purification of cellulases in aqueous two-phase system",
url = "https://hdl.handle.net/21.15107/rcub_dais_139"
}

Antov, M., Jugović, B., Gvozdenović, M. M.,& Knežević Jugović, Z.. (2012). Partitioning and purification of cellulases in aqueous two-phase system. .
https://hdl.handle.net/21.15107/rcub_dais_139

Antov M, Jugović B, Gvozdenović MM, Knežević Jugović Z. Partitioning and purification of cellulases in aqueous two-phase system. 2012;.
https://hdl.handle.net/21.15107/rcub_dais_139 .

Antov, Mirjana, Jugović, Branimir, Gvozdenović, Milica M., Knežević Jugović, Zorica, "Partitioning and purification of cellulases in aqueous two-phase system" (2012),
https://hdl.handle.net/21.15107/rcub_dais_139 .

TY  - JOUR
AU  - Gvozdenović, Milica M.
AU  - Jugović, Branimir
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Knežević Jugović, Zorica
AU  - Grgur, Branimir
PY  - 2011
UR  - https://dais.sanu.ac.rs/123456789/704
AB  - Polyaniline (PANI) enzyme electrode was formed by immobilisation of Glucose oxidase (GOx) via glutaraldehyde into electrochemically polymerised PANI on graphite electrode. Electrochemical polymerisation of PANI on graphite was performed from aqueous solution of 1.0 mol dm−3 HCl and 0.25 mol dm−3 aniline at constant current density of 2.0 mA cm−2. Hronopotentiometric curves of the PANI enzyme electrode obtained at current density of 10 μA cm−2 were recorded in different glucose concentrations. The linearity response range was between 1.0 and 5.0 mmol dm−3 of glucose concentration. The estimated apparent Michaelis–Menten constant, was Km′ = 0.30 mmol dm−3, which is significantly lower than that of free enzyme.
PB  - Elsevier
T2  - Food Chemistry
T1  - Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase
SP  - 396
EP  - 400
DO  - 10.1016/j.foodchem.2010.06.046
UR  - https://hdl.handle.net/21.15107/rcub_dais_704
ER  - 

@article{
author = "Gvozdenović, Milica M. and Jugović, Branimir and Bezbradica, Dejan and Antov, Mirjana and Knežević Jugović, Zorica and Grgur, Branimir",
year = "2011",
abstract = "Polyaniline (PANI) enzyme electrode was formed by immobilisation of Glucose oxidase (GOx) via glutaraldehyde into electrochemically polymerised PANI on graphite electrode. Electrochemical polymerisation of PANI on graphite was performed from aqueous solution of 1.0 mol dm−3 HCl and 0.25 mol dm−3 aniline at constant current density of 2.0 mA cm−2. Hronopotentiometric curves of the PANI enzyme electrode obtained at current density of 10 μA cm−2 were recorded in different glucose concentrations. The linearity response range was between 1.0 and 5.0 mmol dm−3 of glucose concentration. The estimated apparent Michaelis–Menten constant, was Km′ = 0.30 mmol dm−3, which is significantly lower than that of free enzyme.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase",
pages = "396-400",
doi = "10.1016/j.foodchem.2010.06.046",
url = "https://hdl.handle.net/21.15107/rcub_dais_704"
}

Gvozdenović, M. M., Jugović, B., Bezbradica, D., Antov, M., Knežević Jugović, Z.,& Grgur, B.. (2011). Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase. in Food Chemistry
Elsevier., 396-400.
https://doi.org/10.1016/j.foodchem.2010.06.046
https://hdl.handle.net/21.15107/rcub_dais_704

Gvozdenović MM, Jugović B, Bezbradica D, Antov M, Knežević Jugović Z, Grgur B. Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase. in Food Chemistry. 2011;:396-400.
doi:10.1016/j.foodchem.2010.06.046
https://hdl.handle.net/21.15107/rcub_dais_704 .

Gvozdenović, Milica M., Jugović, Branimir, Bezbradica, Dejan, Antov, Mirjana, Knežević Jugović, Zorica, Grgur, Branimir, "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase" in Food Chemistry (2011):396-400,
https://doi.org/10.1016/j.foodchem.2010.06.046 .,
https://hdl.handle.net/21.15107/rcub_dais_704 .

TY  - CONF
AU  - Jambrec, Daliborka
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
AU  - Antov, Mirjana
PY  - 2011
UR  - https://dais.sanu.ac.rs/123456789/694
AB  - A growing interest in biosensors for use in medical, environmental and food analysis
has been recognized. Biosensors are devices that transform chemical information, usually the concentration of a specific sample component, into an analytically useful signal. Their selectivity depends on the characteristics of enzyme and biosensors’ response rate and sensitivity on electroconducting polymer used. Glucose oxidase (GOx) is the most widely used enzyme in the field of biosensors because of its high specificity for a commercially important analyte, high turnover number and high stability. On the other side, among the conducting polyheterocyclic polymers, polypyrolle (PPy) is of particular interest because the relatively low oxidation potential of the monomer enables films to be grown from aqueous solutions that are compatible with most of biological elements. The aim of this study was to investigate the possibility of glucose determination using enzyme electrode obtained by immobilization of GOx into polypyrolle electrochemically polymerised on platinum electrode. Electrochemical synthesis was performed in 0.5 mol dm-3 HCl and 0.2 mol dm-3 pyrolle at constant current density of 2 mA cm-2. Polypyrolle/enzyme electrode was formed by immobilization of glucose oxidase via glutaraldehyde into electrochemically synthesized polypyrolle on platinum electrode. Apparent Michaelis constant was determined and it was found to be 0.045 mmol dm-3, which is much lower than that of free enzyme indicating enhanced enzyme efficiency when it is immobilized into polymer electroconducting matrix. PPy/enzyme electrode lost 5% and 18% of its initial signal after 5 and 20 days, respectively.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering
T1  - Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose
SP  - 1310
EP  - 1310
UR  - https://hdl.handle.net/21.15107/rcub_dais_694
ER  - 

@conference{
author = "Jambrec, Daliborka and Jugović, Branimir and Gvozdenović, Milica M. and Knežević Jugović, Zorica and Antov, Mirjana",
year = "2011",
abstract = "A growing interest in biosensors for use in medical, environmental and food analysis
has been recognized. Biosensors are devices that transform chemical information, usually the concentration of a specific sample component, into an analytically useful signal. Their selectivity depends on the characteristics of enzyme and biosensors’ response rate and sensitivity on electroconducting polymer used. Glucose oxidase (GOx) is the most widely used enzyme in the field of biosensors because of its high specificity for a commercially important analyte, high turnover number and high stability. On the other side, among the conducting polyheterocyclic polymers, polypyrolle (PPy) is of particular interest because the relatively low oxidation potential of the monomer enables films to be grown from aqueous solutions that are compatible with most of biological elements. The aim of this study was to investigate the possibility of glucose determination using enzyme electrode obtained by immobilization of GOx into polypyrolle electrochemically polymerised on platinum electrode. Electrochemical synthesis was performed in 0.5 mol dm-3 HCl and 0.2 mol dm-3 pyrolle at constant current density of 2 mA cm-2. Polypyrolle/enzyme electrode was formed by immobilization of glucose oxidase via glutaraldehyde into electrochemically synthesized polypyrolle on platinum electrode. Apparent Michaelis constant was determined and it was found to be 0.045 mmol dm-3, which is much lower than that of free enzyme indicating enhanced enzyme efficiency when it is immobilized into polymer electroconducting matrix. PPy/enzyme electrode lost 5% and 18% of its initial signal after 5 and 20 days, respectively.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering",
title = "Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose",
pages = "1310-1310",
url = "https://hdl.handle.net/21.15107/rcub_dais_694"
}

Jambrec, D., Jugović, B., Gvozdenović, M. M., Knežević Jugović, Z.,& Antov, M.. (2011). Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose. in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1310-1310.
https://hdl.handle.net/21.15107/rcub_dais_694

Jambrec D, Jugović B, Gvozdenović MM, Knežević Jugović Z, Antov M. Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose. in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering. 2011;:1310-1310.
https://hdl.handle.net/21.15107/rcub_dais_694 .

Jambrec, Daliborka, Jugović, Branimir, Gvozdenović, Milica M., Knežević Jugović, Zorica, Antov, Mirjana, "Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose" in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering (2011):1310-1310,
https://hdl.handle.net/21.15107/rcub_dais_694 .

TY  - CONF
AU  - Knežević Jugović, Zorica
AU  - Jugović, Branimir
AU  - Jakovetić, Sonja
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Saied, Omar Ali
AU  - Gvozdenović, Milica M.
PY  - 2011
UR  - https://dais.sanu.ac.rs/123456789/549
AB  - The present study compares the results of two different methods employed for preparation of polyaniline based glucose biosensor with respect to enzyme loading, biosensing efficiency and potential stability. Kinetic analysis of the potentiometric data for two enzyme immobilized electrode systems show that the GOx/PANI electrode is suitable for assaying samples with low analyte concentrations, whereas the GOx/m-ABA/PANI electrode system exhibits a better potential stability. It may therefore be possible to achieve high level of biosensing efficiency by chemical modeling and synthesis combined with careful selection of the immobilization method.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering
T1  - Design of a polyaniline based biosensor electrode for glucose: A comparative study of two immobilized systems
SP  - 1519
EP  - 1525
UR  - https://hdl.handle.net/21.15107/rcub_dais_549
ER  - 

@conference{
author = "Knežević Jugović, Zorica and Jugović, Branimir and Jakovetić, Sonja and Bezbradica, Dejan and Antov, Mirjana and Saied, Omar Ali and Gvozdenović, Milica M.",
year = "2011",
abstract = "The present study compares the results of two different methods employed for preparation of polyaniline based glucose biosensor with respect to enzyme loading, biosensing efficiency and potential stability. Kinetic analysis of the potentiometric data for two enzyme immobilized electrode systems show that the GOx/PANI electrode is suitable for assaying samples with low analyte concentrations, whereas the GOx/m-ABA/PANI electrode system exhibits a better potential stability. It may therefore be possible to achieve high level of biosensing efficiency by chemical modeling and synthesis combined with careful selection of the immobilization method.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering",
title = "Design of a polyaniline based biosensor electrode for glucose: A comparative study of two immobilized systems",
pages = "1519-1525",
url = "https://hdl.handle.net/21.15107/rcub_dais_549"
}

Knežević Jugović, Z., Jugović, B., Jakovetić, S., Bezbradica, D., Antov, M., Saied, O. A.,& Gvozdenović, M. M.. (2011). Design of a polyaniline based biosensor electrode for glucose: A comparative study of two immobilized systems. in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1519-1525.
https://hdl.handle.net/21.15107/rcub_dais_549

Knežević Jugović Z, Jugović B, Jakovetić S, Bezbradica D, Antov M, Saied OA, Gvozdenović MM. Design of a polyaniline based biosensor electrode for glucose: A comparative study of two immobilized systems. in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering. 2011;:1519-1525.
https://hdl.handle.net/21.15107/rcub_dais_549 .

Knežević Jugović, Zorica, Jugović, Branimir, Jakovetić, Sonja, Bezbradica, Dejan, Antov, Mirjana, Saied, Omar Ali, Gvozdenović, Milica M., "Design of a polyaniline based biosensor electrode for glucose: A comparative study of two immobilized systems" in Proceedings of the 38th International Conference of Slovak Society of Chemical Engineering (2011):1519-1525,
https://hdl.handle.net/21.15107/rcub_dais_549 .

TY  - CONF
AU  - Jambrec, Daliborka
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Knežević Jugović, Zorica
AU  - Antov, Mirjana
PY  - 2011
UR  - https://dais.sanu.ac.rs/123456789/147
AB  - Poster presented at the 38th International Conference of SSCHE, Tatranske Matliare, Slovakia, May 23–27, 2011
T1  - Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose
UR  - https://hdl.handle.net/21.15107/rcub_dais_147
ER  - 

@conference{
author = "Jambrec, Daliborka and Jugović, Branimir and Gvozdenović, Milica M. and Knežević Jugović, Zorica and Antov, Mirjana",
year = "2011",
abstract = "Poster presented at the 38th International Conference of SSCHE, Tatranske Matliare, Slovakia, May 23–27, 2011",
title = "Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose",
url = "https://hdl.handle.net/21.15107/rcub_dais_147"
}

Jambrec, D., Jugović, B., Gvozdenović, M. M., Knežević Jugović, Z.,& Antov, M.. (2011). Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose. .
https://hdl.handle.net/21.15107/rcub_dais_147

Jambrec D, Jugović B, Gvozdenović MM, Knežević Jugović Z, Antov M. Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose. 2011;.
https://hdl.handle.net/21.15107/rcub_dais_147 .

Jambrec, Daliborka, Jugović, Branimir, Gvozdenović, Milica M., Knežević Jugović, Zorica, Antov, Mirjana, "Polypyrolle/glucose oxidase electrode for electrochemical determination of glucose" (2011),
https://hdl.handle.net/21.15107/rcub_dais_147 .

TY  - JOUR
AU  - Bezbradica, Dejan
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Jakovetić, Sonja
AU  - Knežević Jugović, Zorica
PY  - 2011
UR  - https://dais.sanu.ac.rs/123456789/702
AB  - Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml−1. Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.
PB  - Elsevier
T2  - Journal of Molecular Catalysis B: Enzymatic
T1  - Electrochemically synthesized polyaniline as support for lipase immobilization
SP  - 55
EP  - 60
DO  - 10.1016/j.molcatb.2011.02.004
UR  - https://hdl.handle.net/21.15107/rcub_dais_702
ER  - 

@article{
author = "Bezbradica, Dejan and Jugović, Branimir and Gvozdenović, Milica M. and Jakovetić, Sonja and Knežević Jugović, Zorica",
year = "2011",
abstract = "Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml−1. Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.",
publisher = "Elsevier",
journal = "Journal of Molecular Catalysis B: Enzymatic",
title = "Electrochemically synthesized polyaniline as support for lipase immobilization",
pages = "55-60",
doi = "10.1016/j.molcatb.2011.02.004",
url = "https://hdl.handle.net/21.15107/rcub_dais_702"
}

Bezbradica, D., Jugović, B., Gvozdenović, M. M., Jakovetić, S.,& Knežević Jugović, Z.. (2011). Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B: Enzymatic
Elsevier., 55-60.
https://doi.org/10.1016/j.molcatb.2011.02.004
https://hdl.handle.net/21.15107/rcub_dais_702

Bezbradica D, Jugović B, Gvozdenović MM, Jakovetić S, Knežević Jugović Z. Electrochemically synthesized polyaniline as support for lipase immobilization. in Journal of Molecular Catalysis B: Enzymatic. 2011;:55-60.
doi:10.1016/j.molcatb.2011.02.004
https://hdl.handle.net/21.15107/rcub_dais_702 .

Bezbradica, Dejan, Jugović, Branimir, Gvozdenović, Milica M., Jakovetić, Sonja, Knežević Jugović, Zorica, "Electrochemically synthesized polyaniline as support for lipase immobilization" in Journal of Molecular Catalysis B: Enzymatic (2011):55-60,
https://doi.org/10.1016/j.molcatb.2011.02.004 .,
https://hdl.handle.net/21.15107/rcub_dais_702 .

TY  - CONF
AU  - Gvozdenović, Milica M.
AU  - Jugović, Branimir
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Knežević Jugović, Zorica
AU  - Grgur, Branimir
PY  - 2010
UR  - https://dais.sanu.ac.rs/123456789/3512
AB  - Polyaniline (PANI) enzyme electrode was formed by immobilization of Glucose oxidase (GOx) via glutaraldehyde into electrochemicaly polymerized PANI on graphite electrode. Electrochemical polymerization of PANI on graphite was performed from aqueous solution of 1.0 mol dm-3 HCl and 0.25 mol dm-3 aniline at constant current density of 2.0 mA cm-2. Hronopotentiometric curves of the PANI enzyme electrode obtained at current density of 10 μA cm-2 were recorded in different glucose concentrations. The linearity response range was between 1.0-5.0 mmol dm-3 of glucose concentration. The estimated apparent Michaelis-Menten constant, was Km ′ = 0.30 mmol dm-3, which is scientifically lower than that of free enzyme.
PB  - Nice : International Society of Electrochemistry
C3  - The 61st Annual Meeting of the International Society of Electrochemistry: Electrochemistry from Biology to Physics September 26th - October 1st, 2010, Nice, France: Book of Abstracts
T1  - Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize
VL  - s11-P-041
UR  - https://hdl.handle.net/21.15107/rcub_dais_3512
ER  - 

@conference{
author = "Gvozdenović, Milica M. and Jugović, Branimir and Bezbradica, Dejan and Antov, Mirjana and Knežević Jugović, Zorica and Grgur, Branimir",
year = "2010",
abstract = "Polyaniline (PANI) enzyme electrode was formed by immobilization of Glucose oxidase (GOx) via glutaraldehyde into electrochemicaly polymerized PANI on graphite electrode. Electrochemical polymerization of PANI on graphite was performed from aqueous solution of 1.0 mol dm-3 HCl and 0.25 mol dm-3 aniline at constant current density of 2.0 mA cm-2. Hronopotentiometric curves of the PANI enzyme electrode obtained at current density of 10 μA cm-2 were recorded in different glucose concentrations. The linearity response range was between 1.0-5.0 mmol dm-3 of glucose concentration. The estimated apparent Michaelis-Menten constant, was Km ′ = 0.30 mmol dm-3, which is scientifically lower than that of free enzyme.",
publisher = "Nice : International Society of Electrochemistry",
journal = "The 61st Annual Meeting of the International Society of Electrochemistry: Electrochemistry from Biology to Physics September 26th - October 1st, 2010, Nice, France: Book of Abstracts",
title = "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize",
volume = "s11-P-041",
url = "https://hdl.handle.net/21.15107/rcub_dais_3512"
}

Gvozdenović, M. M., Jugović, B., Bezbradica, D., Antov, M., Knežević Jugović, Z.,& Grgur, B.. (2010). Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize. in The 61st Annual Meeting of the International Society of Electrochemistry: Electrochemistry from Biology to Physics September 26th - October 1st, 2010, Nice, France: Book of Abstracts
Nice : International Society of Electrochemistry., s11-P-041.
https://hdl.handle.net/21.15107/rcub_dais_3512

Gvozdenović MM, Jugović B, Bezbradica D, Antov M, Knežević Jugović Z, Grgur B. Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize. in The 61st Annual Meeting of the International Society of Electrochemistry: Electrochemistry from Biology to Physics September 26th - October 1st, 2010, Nice, France: Book of Abstracts. 2010;s11-P-041.
https://hdl.handle.net/21.15107/rcub_dais_3512 .

Gvozdenović, Milica M., Jugović, Branimir, Bezbradica, Dejan, Antov, Mirjana, Knežević Jugović, Zorica, Grgur, Branimir, "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize" in The 61st Annual Meeting of the International Society of Electrochemistry: Electrochemistry from Biology to Physics September 26th - October 1st, 2010, Nice, France: Book of Abstracts, s11-P-041 (2010),
https://hdl.handle.net/21.15107/rcub_dais_3512 .