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  - 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  - Jambrec, Daliborka
AU  - Gvozdenović, Milica M.
AU  - Antov, Mirjana
AU  - Grgur, Branimir
AU  - Jokić, Bojan
AU  - Stevanović, Jasmina S.
AU  - Jugović, Branimir
PY  - 2012
UR  - https://dais.sanu.ac.rs/123456789/469
AB  - Electrochemical deposition of polyaniline (PANI) on graphite electrode was performed galvanostaticaly at constant current density in the range of 1.0 – 5.0 mA cm-2 from aqueous acidic electrolyte containing aniline monomer. Based on ratio of doping/dedoping
charge capacities, it was estimated that current density of 2.0 mA cm-2 was optimal. The structure of the electrochemically synthesized PANI was fibrous, uniform and three dimensional with highly developed surface. Immobilization of glucose oxidise (GOx) was achieved by cross linking via glutaraldehyde and the efficiency of the immobilization was determined spectrophotometrically. Chronoamperometric curves were recorded at different glucose concentrations and used to estimate the apparent Michaelis constant, which was shown to be 0.27 mM. The storage stability of the PANI enzyme electrode was also estimated.
PB  - Bucharest : National Institute of Materials Physics
T2  - Digest journal of nanomaterials and biostructures
T1  - Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose
SP  - 785
EP  - 794
UR  - https://hdl.handle.net/21.15107/rcub_dais_469
ER  - 

@article{
author = "Jambrec, Daliborka and Gvozdenović, Milica M. and Antov, Mirjana and Grgur, Branimir and Jokić, Bojan and Stevanović, Jasmina S. and Jugović, Branimir",
year = "2012",
abstract = "Electrochemical deposition of polyaniline (PANI) on graphite electrode was performed galvanostaticaly at constant current density in the range of 1.0 – 5.0 mA cm-2 from aqueous acidic electrolyte containing aniline monomer. Based on ratio of doping/dedoping
charge capacities, it was estimated that current density of 2.0 mA cm-2 was optimal. The structure of the electrochemically synthesized PANI was fibrous, uniform and three dimensional with highly developed surface. Immobilization of glucose oxidise (GOx) was achieved by cross linking via glutaraldehyde and the efficiency of the immobilization was determined spectrophotometrically. Chronoamperometric curves were recorded at different glucose concentrations and used to estimate the apparent Michaelis constant, which was shown to be 0.27 mM. The storage stability of the PANI enzyme electrode was also estimated.",
publisher = "Bucharest : National Institute of Materials Physics",
journal = "Digest journal of nanomaterials and biostructures",
title = "Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose",
pages = "785-794",
url = "https://hdl.handle.net/21.15107/rcub_dais_469"
}

Jambrec, D., Gvozdenović, M. M., Antov, M., Grgur, B., Jokić, B., Stevanović, J. S.,& Jugović, B.. (2012). Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose. in Digest journal of nanomaterials and biostructures
Bucharest : National Institute of Materials Physics., 785-794.
https://hdl.handle.net/21.15107/rcub_dais_469

Jambrec D, Gvozdenović MM, Antov M, Grgur B, Jokić B, Stevanović JS, Jugović B. Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose. in Digest journal of nanomaterials and biostructures. 2012;:785-794.
https://hdl.handle.net/21.15107/rcub_dais_469 .

Jambrec, Daliborka, Gvozdenović, Milica M., Antov, Mirjana, Grgur, Branimir, Jokić, Bojan, Stevanović, Jasmina S., Jugović, Branimir, "Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose" in Digest journal of nanomaterials and biostructures (2012):785-794,
https://hdl.handle.net/21.15107/rcub_dais_469 .

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  - 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 .