TY  - JOUR
AU  - Knežević-Jugović, Zorica
AU  - Culetu, Alina
AU  - Mijalković, Jelena
AU  - Duta, Denisa
AU  - Stefanović, Andrea
AU  - Šekuljica, Nataša
AU  - Đorđević, Verica
AU  - Antov, Mirjana
PY  - 2023
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5560
AB  - Soy protein concentrate (SPC) was hydrolyzed using several commercial food-grade proteases (Alcalase, Neutrase, papain, Everlase, Umamizyme, Flavourzyme) and their combination to obtain promising ingredients in the manufacture of functional bakery products. In all cases, the hydrolysis caused nutritional, sensory, and rheological changes in SPC, as well as protein structural changes like increased surface hydrophobicity and content of exposed SH groups with the magnitude of these changes depending on enzyme specificity. The hydrolysis with the combination of Neutrase and Flavourzyme (NeuFlav) increased essential amino acid content by 9.8% and that of Lys by 32.6% compared to SPC. This hydrolysate showed also significant antioxidant activities including ABTS and superoxide anion scavenging activity and metal-chelating ability. The addition of all hydrolysates in wheat flour decreased water adsorption and increased development time to some extent due to gluten network weakening, but also decreased the rate of starch retrogradation, contributing to the increase of the shelf-life of bakery products. The NeuFlav tasted less bitter than other hydrolysates, while E-nose provided a discrimination index of 93 between control and hydrolysates. It appeared that the addition of the NeuFlav hydrolysate in a cookie formulation improved protein content and nutritional quality and directed to its higher general consumer acceptability than cookies formulated with only wheat flour.
PB  - MDPI
T2  - Foods
T1  - Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies
IS  - 1
SP  - 24
VL  - 12
DO  - 10.3390/foods12010024
ER  - 

@article{
author = "Knežević-Jugović, Zorica and Culetu, Alina and Mijalković, Jelena and Duta, Denisa and Stefanović, Andrea and Šekuljica, Nataša and Đorđević, Verica and Antov, Mirjana",
year = "2023",
abstract = "Soy protein concentrate (SPC) was hydrolyzed using several commercial food-grade proteases (Alcalase, Neutrase, papain, Everlase, Umamizyme, Flavourzyme) and their combination to obtain promising ingredients in the manufacture of functional bakery products. In all cases, the hydrolysis caused nutritional, sensory, and rheological changes in SPC, as well as protein structural changes like increased surface hydrophobicity and content of exposed SH groups with the magnitude of these changes depending on enzyme specificity. The hydrolysis with the combination of Neutrase and Flavourzyme (NeuFlav) increased essential amino acid content by 9.8% and that of Lys by 32.6% compared to SPC. This hydrolysate showed also significant antioxidant activities including ABTS and superoxide anion scavenging activity and metal-chelating ability. The addition of all hydrolysates in wheat flour decreased water adsorption and increased development time to some extent due to gluten network weakening, but also decreased the rate of starch retrogradation, contributing to the increase of the shelf-life of bakery products. The NeuFlav tasted less bitter than other hydrolysates, while E-nose provided a discrimination index of 93 between control and hydrolysates. It appeared that the addition of the NeuFlav hydrolysate in a cookie formulation improved protein content and nutritional quality and directed to its higher general consumer acceptability than cookies formulated with only wheat flour.",
publisher = "MDPI",
journal = "Foods",
title = "Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies",
number = "1",
pages = "24",
volume = "12",
doi = "10.3390/foods12010024"
}

Knežević-Jugović, Z., Culetu, A., Mijalković, J., Duta, D., Stefanović, A., Šekuljica, N., Đorđević, V.,& Antov, M.. (2023). Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies. in Foods
MDPI., 12(1), 24.
https://doi.org/10.3390/foods12010024

Knežević-Jugović Z, Culetu A, Mijalković J, Duta D, Stefanović A, Šekuljica N, Đorđević V, Antov M. Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies. in Foods. 2023;12(1):24.
doi:10.3390/foods12010024 .

Knežević-Jugović, Zorica, Culetu, Alina, Mijalković, Jelena, Duta, Denisa, Stefanović, Andrea, Šekuljica, Nataša, Đorđević, Verica, Antov, Mirjana, "Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies" in Foods, 12, no. 1 (2023):24,
https://doi.org/10.3390/foods12010024 . .

TY  - JOUR
AU  - Knežević-Jugović, Zorica
AU  - Grbavčić, Sanja
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Bezbradica, Dejan
AU  - Mijin, Dušan
AU  - Antov, Mirjana
PY  - 2017
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3499
AB  - A selection of best combination of adequate immobilization support and efficient immobilization method is still a key requirement for successful application of immobilized enzymes on an industrial level. Eupergit® supports exhibit good mechanical and chemical properties and allow establishment of satisfactory hydrodynamic regime in enzyme reactors. This is advantageous for their wide application in enzyme immobilization after finding the most favorable immobilization method. Methods for enzyme immobilization that have been previously reported as efficient considering the obtained activity of immobilized enzyme are presented: direct binding to polymers via their epoxy groups, binding to polymers via a spacer made from ethylene diamine/glutaraldehyde, and coupling the periodate-oxidized sugar moieties of the enzymes to the polymer beads. The modification of the conventionally immobilized enzyme with ethylenediamine via the carbodiimide route seems to be a powerful tool to improve its stability and catalytic activity.
T2  - Methods in Molecular Biology
T1  - Covalent immobilization of enzymes on Eupergit® supports: Effect of the immobilization protocol
EP  - 91
SP  - 75
VL  - 1504
DO  - 10.1007/978-1-4939-6499-4_7
ER  - 

@article{
author = "Knežević-Jugović, Zorica and Grbavčić, Sanja and Jovanović, Jelena and Stefanović, Andrea and Bezbradica, Dejan and Mijin, Dušan and Antov, Mirjana",
year = "2017",
abstract = "A selection of best combination of adequate immobilization support and efficient immobilization method is still a key requirement for successful application of immobilized enzymes on an industrial level. Eupergit® supports exhibit good mechanical and chemical properties and allow establishment of satisfactory hydrodynamic regime in enzyme reactors. This is advantageous for their wide application in enzyme immobilization after finding the most favorable immobilization method. Methods for enzyme immobilization that have been previously reported as efficient considering the obtained activity of immobilized enzyme are presented: direct binding to polymers via their epoxy groups, binding to polymers via a spacer made from ethylene diamine/glutaraldehyde, and coupling the periodate-oxidized sugar moieties of the enzymes to the polymer beads. The modification of the conventionally immobilized enzyme with ethylenediamine via the carbodiimide route seems to be a powerful tool to improve its stability and catalytic activity.",
journal = "Methods in Molecular Biology",
title = "Covalent immobilization of enzymes on Eupergit® supports: Effect of the immobilization protocol",
pages = "91-75",
volume = "1504",
doi = "10.1007/978-1-4939-6499-4_7"
}

Knežević-Jugović, Z., Grbavčić, S., Jovanović, J., Stefanović, A., Bezbradica, D., Mijin, D.,& Antov, M.. (2017). Covalent immobilization of enzymes on Eupergit® supports: Effect of the immobilization protocol. in Methods in Molecular Biology, 1504, 75-91.
https://doi.org/10.1007/978-1-4939-6499-4_7

Knežević-Jugović Z, Grbavčić S, Jovanović J, Stefanović A, Bezbradica D, Mijin D, Antov M. Covalent immobilization of enzymes on Eupergit® supports: Effect of the immobilization protocol. in Methods in Molecular Biology. 2017;1504:75-91.
doi:10.1007/978-1-4939-6499-4_7 .

Knežević-Jugović, Zorica, Grbavčić, Sanja, Jovanović, Jelena, Stefanović, Andrea, Bezbradica, Dejan, Mijin, Dušan, Antov, Mirjana, "Covalent immobilization of enzymes on Eupergit® supports: Effect of the immobilization protocol" in Methods in Molecular Biology, 1504 (2017):75-91,
https://doi.org/10.1007/978-1-4939-6499-4_7 . .

TY  - JOUR
AU  - Jugović, Branimir
AU  - Grgur, Branimir
AU  - Antov, Mirjana
AU  - Knežević-Jugović, Zorica
AU  - Stevanović, Jasmina
AU  - Gvozdenović, Milica
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3184
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.
PB  - Electrochemical Science Group, Beograd
T2  - International Journal of Electrochemical Science
T1  - Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose
EP  - 1161
IS  - 2
SP  - 1152
VL  - 11
UR  - https://hdl.handle.net/21.15107/rcub_technorep_3184
ER  - 

@article{
author = "Jugović, Branimir and Grgur, Branimir and Antov, Mirjana and Knežević-Jugović, Zorica and Stevanović, Jasmina and Gvozdenović, Milica",
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.",
publisher = "Electrochemical Science Group, Beograd",
journal = "International Journal of Electrochemical Science",
title = "Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose",
pages = "1161-1152",
number = "2",
volume = "11",
url = "https://hdl.handle.net/21.15107/rcub_technorep_3184"
}

Jugović, B., Grgur, B., Antov, M., Knežević-Jugović, Z., Stevanović, J.,& Gvozdenović, M.. (2016). Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose. in International Journal of Electrochemical Science
Electrochemical Science Group, Beograd., 11(2), 1152-1161.
https://hdl.handle.net/21.15107/rcub_technorep_3184

Jugović B, Grgur B, Antov M, Knežević-Jugović Z, Stevanović J, Gvozdenović M. Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose. in International Journal of Electrochemical Science. 2016;11(2):1152-1161.
https://hdl.handle.net/21.15107/rcub_technorep_3184 .

Jugović, Branimir, Grgur, Branimir, Antov, Mirjana, Knežević-Jugović, Zorica, Stevanović, Jasmina, Gvozdenović, Milica, "Polypyrrole-based Enzyme Electrode with Immobilized Glucose Oxidase for Electrochemical Determination of Glucose" in International Journal of Electrochemical Science, 11, no. 2 (2016):1152-1161,
https://hdl.handle.net/21.15107/rcub_technorep_3184 .

TY  - JOUR
AU  - Antov, Mirjana
AU  - Ivetić, Darjana Z.
AU  - Knežević-Jugović, Zorica
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3438
AB  - Recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction was studied with maximal possible crude enzyme loads. In polyethylene glycol/dextran and polyethylene glycol/salt systems the influences of molecular weight and concentration of polyethylene glycol, phase-forming salt and phase volume ratio were evaluated. Lipase partition coefficient 9 followed by the top phase yield 95.7% and purification factor 3.4 were achieved in 15% (w w(-1)) polyethylene glycol 4000/15% (w w(-1)) KH2PO4/70% (w w(-1)) crude enzyme. Efficient single-step recovery of lipase followed by partial enzyme purification indicated possible integration of production and primary bioseparation step by aqueous two-phase extraction. By varying phase volume ratio, the concentration of phosphate was reduced without decrease in lipase recovery.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Separation Science and Technology
T1  - Single step recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction
EP  - 628
IS  - 4
SP  - 622
VL  - 51
DO  - 10.1080/01496395.2015.1117106
ER  - 

@article{
author = "Antov, Mirjana and Ivetić, Darjana Z. and Knežević-Jugović, Zorica",
year = "2016",
abstract = "Recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction was studied with maximal possible crude enzyme loads. In polyethylene glycol/dextran and polyethylene glycol/salt systems the influences of molecular weight and concentration of polyethylene glycol, phase-forming salt and phase volume ratio were evaluated. Lipase partition coefficient 9 followed by the top phase yield 95.7% and purification factor 3.4 were achieved in 15% (w w(-1)) polyethylene glycol 4000/15% (w w(-1)) KH2PO4/70% (w w(-1)) crude enzyme. Efficient single-step recovery of lipase followed by partial enzyme purification indicated possible integration of production and primary bioseparation step by aqueous two-phase extraction. By varying phase volume ratio, the concentration of phosphate was reduced without decrease in lipase recovery.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Separation Science and Technology",
title = "Single step recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction",
pages = "628-622",
number = "4",
volume = "51",
doi = "10.1080/01496395.2015.1117106"
}

Antov, M., Ivetić, D. Z.,& Knežević-Jugović, Z.. (2016). Single step recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction. in Separation Science and Technology
Taylor & Francis Inc, Philadelphia., 51(4), 622-628.
https://doi.org/10.1080/01496395.2015.1117106

Antov M, Ivetić DZ, Knežević-Jugović Z. Single step recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction. in Separation Science and Technology. 2016;51(4):622-628.
doi:10.1080/01496395.2015.1117106 .

Antov, Mirjana, Ivetić, Darjana Z., Knežević-Jugović, Zorica, "Single step recovery of lipase from Penicillium cyclopium by aqueous two-phase extraction" in Separation Science and Technology, 51, no. 4 (2016):622-628,
https://doi.org/10.1080/01496395.2015.1117106 . .

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

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

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

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

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

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Mijin, Dušan
AU  - Knežević-Jugović, Zorica
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2420
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, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica
EP  - 1573
IS  - 7
SP  - 1560
VL  - 170
DO  - 10.1007/s12010-013-0294-z
ER  - 

@article{
author = "Jakovetić, Sonja and Jugović, Branimir and Gvozdenović, Milica 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, New York",
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 = "1573-1560",
number = "7",
volume = "170",
doi = "10.1007/s12010-013-0294-z"
}

Jakovetić, S., Jugović, B., Gvozdenović, 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, New York., 170(7), 1560-1573.
https://doi.org/10.1007/s12010-013-0294-z

Jakovetić S, Jugović B, Gvozdenović M, 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 .

Jakovetić, Sonja, Jugović, Branimir, Gvozdenović, Milica, 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 . .

TY  - CONF
AU  - Knežević-Jugović, Zorica
AU  - Gluvić, Ana
AU  - Žuža, Milena
AU  - Stefanović, Andrea
AU  - Gvozdenović, Milica
AU  - Jugović, Branimir
AU  - Antov, Mirjana
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2279
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
EP  - 1439
SP  - 1433
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2279
ER  - 

@conference{
author = "Knežević-Jugović, Zorica and Gluvić, Ana and Žuža, Milena and Stefanović, Andrea and Gvozdenović, Milica 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 = "1439-1433",
url = "https://hdl.handle.net/21.15107/rcub_technorep_2279"
}

Knežević-Jugović, Z., Gluvić, A., Žuža, M., Stefanović, A., Gvozdenović, 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_technorep_2279

Knežević-Jugović Z, Gluvić A, Žuža M, Stefanović A, Gvozdenović M, 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_technorep_2279 .

Knežević-Jugović, Zorica, Gluvić, Ana, Žuža, Milena, Stefanović, Andrea, Gvozdenović, Milica, 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_technorep_2279 .

TY  - CONF
AU  - Knežević-Jugović, Zorica
AU  - Jakovetić, Sonja
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Grbavčić, Sanja
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2019
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
EP  - 1432
SP  - 1426
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2019
ER  - 

@conference{
author = "Knežević-Jugović, Zorica and Jakovetić, Sonja and Jugović, Branimir and Gvozdenović, Milica 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 = "1432-1426",
url = "https://hdl.handle.net/21.15107/rcub_technorep_2019"
}

Knežević-Jugović, Z., Jakovetić, S., Jugović, B., Gvozdenović, 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_technorep_2019

Knežević-Jugović Z, Jakovetić S, Jugović B, Gvozdenović M, 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_technorep_2019 .

Knežević-Jugović, Zorica, Jakovetić, Sonja, Jugović, Branimir, Gvozdenović, Milica, 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_technorep_2019 .

TY  - CONF
AU  - Antov, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2015
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
EP  - 1346
SP  - 1346
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2015
ER  - 

@conference{
author = "Antov, Mirjana and Jugović, Branimir and Gvozdenović, Milica 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_technorep_2015"
}

Antov, M., Jugović, B., Gvozdenović, 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_technorep_2015

Antov M, Jugović B, Gvozdenović M, 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_technorep_2015 .

Antov, Mirjana, Jugović, Branimir, Gvozdenović, Milica, 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_technorep_2015 .

TY  - JOUR
AU  - Jambrec, Daliborka
AU  - Gvozdenović, Milica
AU  - Antov, Mirjana
AU  - Grgur, Branimir
AU  - Jokić, Bojan
AU  - Stevanović, Jasmina
AU  - Jugović, Branimir
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2136
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  - Inst Materials Physics, Bucharest
T2  - Digest Journal of Nanomaterials and Biostructures
T1  - Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose
EP  - 794
IS  - 2
SP  - 785
VL  - 7
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2136
ER  - 

@article{
author = "Jambrec, Daliborka and Gvozdenović, Milica and Antov, Mirjana and Grgur, Branimir and Jokić, Bojan and Stevanović, Jasmina 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 = "Inst Materials Physics, Bucharest",
journal = "Digest Journal of Nanomaterials and Biostructures",
title = "Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose",
pages = "794-785",
number = "2",
volume = "7",
url = "https://hdl.handle.net/21.15107/rcub_technorep_2136"
}

Jambrec, D., Gvozdenović, M., Antov, M., Grgur, B., Jokić, B., Stevanović, J.,& Jugović, B.. (2012). Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose. in Digest Journal of Nanomaterials and Biostructures
Inst Materials Physics, Bucharest., 7(2), 785-794.
https://hdl.handle.net/21.15107/rcub_technorep_2136

Jambrec D, Gvozdenović M, Antov M, Grgur B, Jokić B, Stevanović J, Jugović B. Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose. in Digest Journal of Nanomaterials and Biostructures. 2012;7(2):785-794.
https://hdl.handle.net/21.15107/rcub_technorep_2136 .

Jambrec, Daliborka, Gvozdenović, Milica, Antov, Mirjana, Grgur, Branimir, Jokić, Bojan, Stevanović, Jasmina, Jugović, Branimir, "Electrochemically deposited nano fibrous polyanilne for amperometric determination of glucose" in Digest Journal of Nanomaterials and Biostructures, 7, no. 2 (2012):785-794,
https://hdl.handle.net/21.15107/rcub_technorep_2136 .

TY  - JOUR
AU  - Antov, Mirjana
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2032
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.
AB  - U radu je ispitana raspodela celulolitičke aktivnosti u vodenim dvofaznim sistemima polietilenglikol/dekstran. Maksimalno moguć 100% prinos celulolitičke aktivnosti dobijene kultivacijom Penicillium sp. postignut je u dvofaznom sistemu sastava 10% (m/m) polietilenglikol 1500/5% (m/m) dekstran 500000/ 80% (m/m) sirovi enzim na pH 5 u samo jednom koraku ekstrakcije. Dodatak KH2PO4 u koncentraciji 15 mmol/l u ovaj sistem, iako je smanjio raspodelu celulolitičke aktivnosti iz sirovog enzimskog preparata u gornju fazu sistema, poboljšao je faktor prečišćavanja u toj fazi na vrednost 2,6. Razlike u odzivu između celulolitičkih aktivnosti iz dva ispitivana izvora na promene faktora koji utiču na raspodelu mogu se objasniti različitom kompleksošću njihovih matriksa - komercijalnog, delimično prečišćenog, i sirovog neprečišćenog preparata dobijenog kultivacijom. Naime, i prisustvo samih kontaminenata može dodatno uticati na raspodelu enzimske aktivnosti.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems
T1  - Raspodela celulolitičke aktivnosti u dvofaznim sistemima polietilenglikol/dekstran
EP  - 158
IS  - 43
SP  - 151
DO  - 10.2298/APT1243151A
ER  - 

@article{
author = "Antov, Mirjana and Jugović, Branimir and Gvozdenović, Milica 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., U radu je ispitana raspodela celulolitičke aktivnosti u vodenim dvofaznim sistemima polietilenglikol/dekstran. Maksimalno moguć 100% prinos celulolitičke aktivnosti dobijene kultivacijom Penicillium sp. postignut je u dvofaznom sistemu sastava 10% (m/m) polietilenglikol 1500/5% (m/m) dekstran 500000/ 80% (m/m) sirovi enzim na pH 5 u samo jednom koraku ekstrakcije. Dodatak KH2PO4 u koncentraciji 15 mmol/l u ovaj sistem, iako je smanjio raspodelu celulolitičke aktivnosti iz sirovog enzimskog preparata u gornju fazu sistema, poboljšao je faktor prečišćavanja u toj fazi na vrednost 2,6. Razlike u odzivu između celulolitičkih aktivnosti iz dva ispitivana izvora na promene faktora koji utiču na raspodelu mogu se objasniti različitom kompleksošću njihovih matriksa - komercijalnog, delimično prečišćenog, i sirovog neprečišćenog preparata dobijenog kultivacijom. Naime, i prisustvo samih kontaminenata može dodatno uticati na raspodelu enzimske aktivnosti.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems, Raspodela celulolitičke aktivnosti u dvofaznim sistemima polietilenglikol/dekstran",
pages = "158-151",
number = "43",
doi = "10.2298/APT1243151A"
}

Antov, M., Jugović, B., Gvozdenović, M.,& Knežević-Jugović, Z.. (2012). Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. in Acta periodica technologica
Faculty of Technology, Novi Sad.(43), 151-158.
https://doi.org/10.2298/APT1243151A

Antov M, Jugović B, Gvozdenović M, Knežević-Jugović Z. Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems. in Acta periodica technologica. 2012;(43):151-158.
doi:10.2298/APT1243151A .

Antov, Mirjana, Jugović, Branimir, Gvozdenović, Milica, Knežević-Jugović, Zorica, "Partitioning of cellulolytic activity in the polyethylene glycol/dextran two-phase systems" in Acta periodica technologica, no. 43 (2012):151-158,
https://doi.org/10.2298/APT1243151A . .

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
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1768
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
EP  - 1525
SP  - 1519
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1768
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",
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 = "1525-1519",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1768"
}

Knežević-Jugović, Z., Jugović, B., Jakovetić, S., Bezbradica, D., Antov, M., Saied, O. A.,& Gvozdenović, 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_technorep_1768

Knežević-Jugović Z, Jugović B, Jakovetić S, Bezbradica D, Antov M, Saied OA, Gvozdenović 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_technorep_1768 .

Knežević-Jugović, Zorica, Jugović, Branimir, Jakovetić, Sonja, Bezbradica, Dejan, Antov, Mirjana, Saied, Omar Ali, Gvozdenović, Milica, "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_technorep_1768 .

TY  - CONF
AU  - Jambrec, Daliborka
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Knežević-Jugović, Zorica
AU  - Antov, Mirjana
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1769
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
EP  - 1310
SP  - 1310
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1769
ER  - 

@conference{
author = "Jambrec, Daliborka and Jugović, Branimir and Gvozdenović, Milica 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_technorep_1769"
}

Jambrec, D., Jugović, B., Gvozdenović, 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_technorep_1769

Jambrec D, Jugović B, Gvozdenović M, 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_technorep_1769 .

Jambrec, Daliborka, Jugović, Branimir, Gvozdenović, Milica, 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_technorep_1769 .

TY  - JOUR
AU  - Gvozdenović, Milica
AU  - Jugović, Branimir
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Knežević-Jugović, Zorica
AU  - Grgur, Branimir
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1826
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 mu A 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 K-m(') = 0.30 mmol dm(-3), which is significantly lower than that of free enzyme.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase
EP  - 400
IS  - 1
SP  - 396
VL  - 124
DO  - 10.1016/j.foodchem.2010.06.046
ER  - 

@article{
author = "Gvozdenović, Milica 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 mu A 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 K-m(') = 0.30 mmol dm(-3), which is significantly lower than that of free enzyme.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidase",
pages = "400-396",
number = "1",
volume = "124",
doi = "10.1016/j.foodchem.2010.06.046"
}

Gvozdenović, 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 Sci Ltd, Oxford., 124(1), 396-400.
https://doi.org/10.1016/j.foodchem.2010.06.046

Gvozdenović M, 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;124(1):396-400.
doi:10.1016/j.foodchem.2010.06.046 .

Gvozdenović, Milica, 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, 124, no. 1 (2011):396-400,
https://doi.org/10.1016/j.foodchem.2010.06.046 . .

TY  - CONF
AU  - Gvozdenović, Milica
AU  - Jugović, Branimir
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Knežević-Jugović, Zorica
AU  - Grgur, Branimir
PY  - 2010
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1575
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 Biol
T1  - Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize
VL  - s11-P-041
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1575
ER  - 

@conference{
author = "Gvozdenović, Milica 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 Biol",
title = "Electrochemical determination of glucose using polyaniline electrode modified by glucose oxidize",
volume = "s11-P-041",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1575"
}

Gvozdenović, 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 Biol
Nice : International Society of Electrochemistry., s11-P-041.
https://hdl.handle.net/21.15107/rcub_technorep_1575

Gvozdenović M, 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 Biol. 2010;s11-P-041.
https://hdl.handle.net/21.15107/rcub_technorep_1575 .

Gvozdenović, Milica, 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 Biol, s11-P-041 (2010),
https://hdl.handle.net/21.15107/rcub_technorep_1575 .