TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3732
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
VL  - 42
IS  - 24
SP  - 2626
EP  - 2636
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2021",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
volume = "42",
number = "24",
pages = "2626-2636",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2021). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley., 42(24), 2626-2636.
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2021;42(24):2626-2636.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis, 42, no. 24 (2021):2626-2636,
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Lončar, Nikola
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh Padamati
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3052
AB  - Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7–24 h with good yields (70–99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 °C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
VL  - 132
SP  - 109411
DO  - 10.1016/j.enzmictec.2019.109411
ER  - 

@article{
author = "Simić, Stefan and Jeremić, Sanja and Đokić, Lidija and Božić, Nataša and Vujčić, Zoran and Lončar, Nikola and Senthamaraikannan, Ramsankar and Babu, Ramesh Padamati and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7–24 h with good yields (70–99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 °C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines",
volume = "132",
pages = "109411",
doi = "10.1016/j.enzmictec.2019.109411"
}

Simić, S., Jeremić, S., Đokić, L., Božić, N., Vujčić, Z., Lončar, N., Senthamaraikannan, R., Babu, R. P., Opsenica, I.,& Nikodinović-Runić, J.. (2020). Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology
Elsevier., 132, 109411.
https://doi.org/10.1016/j.enzmictec.2019.109411

Simić S, Jeremić S, Đokić L, Božić N, Vujčić Z, Lončar N, Senthamaraikannan R, Babu RP, Opsenica I, Nikodinović-Runić J. Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology. 2020;132:109411.
doi:10.1016/j.enzmictec.2019.109411 .

Simić, Stefan, Jeremić, Sanja, Đokić, Lidija, Božić, Nataša, Vujčić, Zoran, Lončar, Nikola, Senthamaraikannan, Ramsankar, Babu, Ramesh Padamati, Opsenica, Igor, Nikodinović-Runić, Jasmina, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" in Enzyme and Microbial Technology, 132 (2020):109411,
https://doi.org/10.1016/j.enzmictec.2019.109411 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3989
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2020",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2020). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley..
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2020;.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis (2020),
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Lončar, Nikola
AU  - Drašković, Natalija
AU  - Božić, Nataša
AU  - Romero, Elvira
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Vujčić, Zoran
AU  - Fraaije, Marco W.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3021
AB  - The consumption of dyes is increasing worldwide in line with the increase of population
and demand for clothes and other colored products. However, the e ciency of dyeing processes
is still poor and results in large amounts of colored e uents. It is desired to develop a portfolio
of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome
sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (PfDyP B2) could be overexpressed as a soluble protein. PfDyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of PfDyP B2 in calcium-alginate beads resulted in a significant increase in stability: PfDyP B2 retains 80% of its initial activity after 2 h incubation at 50 °C, while the soluble enzyme is inactivated within minutes. PfDyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30 °C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.
PB  - MDPI
T2  - Catalysts
T1  - Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1
VL  - 9
SP  - 463
DO  - 10.3390/catal9050463
ER  - 

@article{
author = "Lončar, Nikola and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
abstract = "The consumption of dyes is increasing worldwide in line with the increase of population
and demand for clothes and other colored products. However, the e ciency of dyeing processes
is still poor and results in large amounts of colored e uents. It is desired to develop a portfolio
of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome
sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (PfDyP B2) could be overexpressed as a soluble protein. PfDyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of PfDyP B2 in calcium-alginate beads resulted in a significant increase in stability: PfDyP B2 retains 80% of its initial activity after 2 h incubation at 50 °C, while the soluble enzyme is inactivated within minutes. PfDyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30 °C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.",
publisher = "MDPI",
journal = "Catalysts",
title = "Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1",
volume = "9",
pages = "463",
doi = "10.3390/catal9050463"
}

Lončar, N., Drašković, N., Božić, N., Romero, E., Simić, S., Opsenica, I., Vujčić, Z.,& Fraaije, M. W.. (2019). Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. in Catalysts
MDPI., 9, 463.
https://doi.org/10.3390/catal9050463

Lončar N, Drašković N, Božić N, Romero E, Simić S, Opsenica I, Vujčić Z, Fraaije MW. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. in Catalysts. 2019;9:463.
doi:10.3390/catal9050463 .

Lončar, Nikola, Drašković, Natalija, Božić, Nataša, Romero, Elvira, Simić, Stefan, Opsenica, Igor, Vujčić, Zoran, Fraaije, Marco W., "Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1" in Catalysts, 9 (2019):463,
https://doi.org/10.3390/catal9050463 . .

TY  - JOUR
AU  - Grujić, Marica
AU  - Dojnov, Biljana
AU  - Potočnik, Ivana
AU  - Atanasova, Lea
AU  - Duduk, Bojan
AU  - Srebotnik, Ewald
AU  - Druzhinina, Irina S.
AU  - Kubicek, Christian P.
AU  - Vujčić, Zoran
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3382
AB  - Lignocellulosic plant biomass is the world’s most abundant carbon source and has consequently attracted attention as a renewable resource for production of biofuels and commodity chemicals that could replace fossil resources. Due to its recalcitrant nature, it must be pretreated by chemical, physical or biological means prior to hydrolysis, introducing additional costs. In this paper, we tested the hypothesis that fungi which thrive on lignocellulosic material (straw, bark or soil) would be efficient in degrading untreated lignocellulose. Wheat straw was used as a model. We developed a fast and simple screening method for cellulase producers and tested one hundred Trichoderma strains isolated from wheat straw. The most potent strain—UB483FTG2/ TUCIM 4455, was isolated from substrate used for mushroom cultivation and was identified as T. guizhouense. After optimization of growth medium, high cellulase activity was already achieved after 72 h of fermentation on raw wheat straw, while the model cellulase overproducing strain T. reesei QM 9414 took 170 h and reached only 45% of the cellulase activity secreted by T. guizhouense. Maximum production levels were 1.1 U/mL (measured with CMC as cellulase substrate) and 0.7 U/mL (β-glucosidase assay). The T. guizhouense cellulase cocktail hydrolyzed raw wheat straw within 35 h. Our study shows that screening for fungi that successfully compete for special substrates in nature will lead to the isolation of strains with qualitatively and quantitatively superior enzymes needed for their digestion which could be used for industrial purposes.
PB  - Springer Science and Business Media LLC
T2  - World Journal of Microbiology and Biotechnology
T1  - Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw
VL  - 35
IS  - 12
SP  - 194
DO  - 10.1007/s11274-019-2774-y
ER  - 

@article{
author = "Grujić, Marica and Dojnov, Biljana and Potočnik, Ivana and Atanasova, Lea and Duduk, Bojan and Srebotnik, Ewald and Druzhinina, Irina S. and Kubicek, Christian P. and Vujčić, Zoran",
year = "2019",
abstract = "Lignocellulosic plant biomass is the world’s most abundant carbon source and has consequently attracted attention as a renewable resource for production of biofuels and commodity chemicals that could replace fossil resources. Due to its recalcitrant nature, it must be pretreated by chemical, physical or biological means prior to hydrolysis, introducing additional costs. In this paper, we tested the hypothesis that fungi which thrive on lignocellulosic material (straw, bark or soil) would be efficient in degrading untreated lignocellulose. Wheat straw was used as a model. We developed a fast and simple screening method for cellulase producers and tested one hundred Trichoderma strains isolated from wheat straw. The most potent strain—UB483FTG2/ TUCIM 4455, was isolated from substrate used for mushroom cultivation and was identified as T. guizhouense. After optimization of growth medium, high cellulase activity was already achieved after 72 h of fermentation on raw wheat straw, while the model cellulase overproducing strain T. reesei QM 9414 took 170 h and reached only 45% of the cellulase activity secreted by T. guizhouense. Maximum production levels were 1.1 U/mL (measured with CMC as cellulase substrate) and 0.7 U/mL (β-glucosidase assay). The T. guizhouense cellulase cocktail hydrolyzed raw wheat straw within 35 h. Our study shows that screening for fungi that successfully compete for special substrates in nature will lead to the isolation of strains with qualitatively and quantitatively superior enzymes needed for their digestion which could be used for industrial purposes.",
publisher = "Springer Science and Business Media LLC",
journal = "World Journal of Microbiology and Biotechnology",
title = "Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw",
volume = "35",
number = "12",
pages = "194",
doi = "10.1007/s11274-019-2774-y"
}

Grujić, M., Dojnov, B., Potočnik, I., Atanasova, L., Duduk, B., Srebotnik, E., Druzhinina, I. S., Kubicek, C. P.,& Vujčić, Z.. (2019). Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw. in World Journal of Microbiology and Biotechnology
Springer Science and Business Media LLC., 35(12), 194.
https://doi.org/10.1007/s11274-019-2774-y

Grujić M, Dojnov B, Potočnik I, Atanasova L, Duduk B, Srebotnik E, Druzhinina IS, Kubicek CP, Vujčić Z. Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw. in World Journal of Microbiology and Biotechnology. 2019;35(12):194.
doi:10.1007/s11274-019-2774-y .

Grujić, Marica, Dojnov, Biljana, Potočnik, Ivana, Atanasova, Lea, Duduk, Bojan, Srebotnik, Ewald, Druzhinina, Irina S., Kubicek, Christian P., Vujčić, Zoran, "Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw" in World Journal of Microbiology and Biotechnology, 35, no. 12 (2019):194,
https://doi.org/10.1007/s11274-019-2774-y . .

TY  - JOUR
AU  - Tadić, Vojin
AU  - Petrić, Marija
AU  - Uzelac, Branka
AU  - Milosevic, Snezana
AU  - Vujčić, Zoran
AU  - Stevanović, Jasmina
AU  - Tadić, Jovan
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2321
AB  - We investigated the removal of phenol from water solutions (200 mg L-1) using two varieties of lettuce (Lactuca sativa L) and their hairy roots. Experiments were done in a hydroponic system where adult plants were grown in phenol solutions for 10 days. The solution was refreshed every two days in order to maintain the constant concentration of phenol. Hairy roots were also cultivated in a solution containing phenol at concentrations varying from 25 to 125 mg L-1 in order to determine the maximum concentration of phenol that can be removed by hairy roots. Both varieties of lettuce reduced the concentration of phenol below the detection limit after six days at the initial phenol concentration of 200 mg L-1. Transformed roots completely removed phenol at the initial concentrations of 100 mg L-1, but were not able to remove phenol at constant concentration above 25 mg L-1. Lettuce plants and hairy roots are excellent candidates for the process of phenol removal from wastewaters. This plant is good choice for bioremediation of water and represents a potentially efficient and inexpensive system for water purification. The performance of lettuce plants and hairy roots to remove phenol from water solutions under real conditions, depleted nutrients or presence of other compounds should be examined further.
PB  - Elsevier
T2  - Scientia Horticulturae
T1  - Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1
VL  - 231
SP  - 210
EP  - 218
DO  - 10.1016/j.scienta.2017.12.025
ER  - 

@article{
author = "Tadić, Vojin and Petrić, Marija and Uzelac, Branka and Milosevic, Snezana and Vujčić, Zoran and Stevanović, Jasmina and Tadić, Jovan",
year = "2018",
abstract = "We investigated the removal of phenol from water solutions (200 mg L-1) using two varieties of lettuce (Lactuca sativa L) and their hairy roots. Experiments were done in a hydroponic system where adult plants were grown in phenol solutions for 10 days. The solution was refreshed every two days in order to maintain the constant concentration of phenol. Hairy roots were also cultivated in a solution containing phenol at concentrations varying from 25 to 125 mg L-1 in order to determine the maximum concentration of phenol that can be removed by hairy roots. Both varieties of lettuce reduced the concentration of phenol below the detection limit after six days at the initial phenol concentration of 200 mg L-1. Transformed roots completely removed phenol at the initial concentrations of 100 mg L-1, but were not able to remove phenol at constant concentration above 25 mg L-1. Lettuce plants and hairy roots are excellent candidates for the process of phenol removal from wastewaters. This plant is good choice for bioremediation of water and represents a potentially efficient and inexpensive system for water purification. The performance of lettuce plants and hairy roots to remove phenol from water solutions under real conditions, depleted nutrients or presence of other compounds should be examined further.",
publisher = "Elsevier",
journal = "Scientia Horticulturae",
title = "Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1",
volume = "231",
pages = "210-218",
doi = "10.1016/j.scienta.2017.12.025"
}

Tadić, V., Petrić, M., Uzelac, B., Milosevic, S., Vujčić, Z., Stevanović, J.,& Tadić, J.. (2018). Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1. in Scientia Horticulturae
Elsevier., 231, 210-218.
https://doi.org/10.1016/j.scienta.2017.12.025

Tadić V, Petrić M, Uzelac B, Milosevic S, Vujčić Z, Stevanović J, Tadić J. Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1. in Scientia Horticulturae. 2018;231:210-218.
doi:10.1016/j.scienta.2017.12.025 .

Tadić, Vojin, Petrić, Marija, Uzelac, Branka, Milosevic, Snezana, Vujčić, Zoran, Stevanović, Jasmina, Tadić, Jovan, "Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1" in Scientia Horticulturae, 231 (2018):210-218,
https://doi.org/10.1016/j.scienta.2017.12.025 . .

TY  - JOUR
AU  - Miocinovic, Jelena
AU  - Tomic, Nikola
AU  - Dojnov, Biljana
AU  - Tomasević, Igor
AU  - Stojanović, Sanja
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2469
AB  - BACKGROUND: The need to increase the daily intake of dietary fibres opens a new chapter in the research of functional foods enriched with fibres. The potential application of an innovative product - insoluble dietary fibres from triticale in yoghurts - was deployed by characterising their food application and evaluating physico-chemical, rheological and sensory properties and was the aim of this research. RESULTS: Detailed characterisations of these fibres are presented for the first time and showed very good hydration properties, optimal pH ( slightly acidic), optimal chemical composition, high antioxidant capacity which was proven by phenolics contents. Besides, these fibres showed negligible calorific value, with no phytates and high antioxidant capacity, mainly from ferulic acid. Therefore they could be successfully added to yoghurt. Enrichment of yoghurt having different milk fat content (1.5 and 2.8% w/w) with triticale insoluble fibre (1.5% and 3.0% w/w) significantly influenced the syneresis level, its apparent viscosity, yield stress and thixotropic behaviour. The overall sensory quality scores indicated that yoghurt enriched with 1.5% triticale insoluble fibres was recognised as 'excellent' and had enhanced antioxidant activity. CONCLUSIONS: Insoluble triticale fibre could therefore be used as a supplement to produce functional yoghurt.
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties
VL  - 98
IS  - 4
SP  - 1291
EP  - 1299
DO  - 10.1002/jsfa.8592
ER  - 

@article{
author = "Miocinovic, Jelena and Tomic, Nikola and Dojnov, Biljana and Tomasević, Igor and Stojanović, Sanja and Đekić, Ilija and Vujčić, Zoran",
year = "2018",
abstract = "BACKGROUND: The need to increase the daily intake of dietary fibres opens a new chapter in the research of functional foods enriched with fibres. The potential application of an innovative product - insoluble dietary fibres from triticale in yoghurts - was deployed by characterising their food application and evaluating physico-chemical, rheological and sensory properties and was the aim of this research. RESULTS: Detailed characterisations of these fibres are presented for the first time and showed very good hydration properties, optimal pH ( slightly acidic), optimal chemical composition, high antioxidant capacity which was proven by phenolics contents. Besides, these fibres showed negligible calorific value, with no phytates and high antioxidant capacity, mainly from ferulic acid. Therefore they could be successfully added to yoghurt. Enrichment of yoghurt having different milk fat content (1.5 and 2.8% w/w) with triticale insoluble fibre (1.5% and 3.0% w/w) significantly influenced the syneresis level, its apparent viscosity, yield stress and thixotropic behaviour. The overall sensory quality scores indicated that yoghurt enriched with 1.5% triticale insoluble fibres was recognised as 'excellent' and had enhanced antioxidant activity. CONCLUSIONS: Insoluble triticale fibre could therefore be used as a supplement to produce functional yoghurt.",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties",
volume = "98",
number = "4",
pages = "1291-1299",
doi = "10.1002/jsfa.8592"
}

Miocinovic, J., Tomic, N., Dojnov, B., Tomasević, I., Stojanović, S., Đekić, I.,& Vujčić, Z.. (2018). Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 98(4), 1291-1299.
https://doi.org/10.1002/jsfa.8592

Miocinovic J, Tomic N, Dojnov B, Tomasević I, Stojanović S, Đekić I, Vujčić Z. Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties. in Journal of the Science of Food and Agriculture. 2018;98(4):1291-1299.
doi:10.1002/jsfa.8592 .

Miocinovic, Jelena, Tomic, Nikola, Dojnov, Biljana, Tomasević, Igor, Stojanović, Sanja, Đekić, Ilija, Vujčić, Zoran, "Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties" in Journal of the Science of Food and Agriculture, 98, no. 4 (2018):1291-1299,
https://doi.org/10.1002/jsfa.8592 . .

TY  - JOUR
AU  - Miocinovic, Jelena
AU  - Tomic, Nikola
AU  - Dojnov, Biljana
AU  - Tomasević, Igor
AU  - Stojanović, Sanja
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2968
AB  - BACKGROUND: The need to increase the daily intake of dietary fibres opens a new chapter in the research of functional foods enriched with fibres. The potential application of an innovative product - insoluble dietary fibres from triticale in yoghurts - was deployed by characterising their food application and evaluating physico-chemical, rheological and sensory properties and was the aim of this research. RESULTS: Detailed characterisations of these fibres are presented for the first time and showed very good hydration properties, optimal pH ( slightly acidic), optimal chemical composition, high antioxidant capacity which was proven by phenolics contents. Besides, these fibres showed negligible calorific value, with no phytates and high antioxidant capacity, mainly from ferulic acid. Therefore they could be successfully added to yoghurt. Enrichment of yoghurt having different milk fat content (1.5 and 2.8% w/w) with triticale insoluble fibre (1.5% and 3.0% w/w) significantly influenced the syneresis level, its apparent viscosity, yield stress and thixotropic behaviour. The overall sensory quality scores indicated that yoghurt enriched with 1.5% triticale insoluble fibres was recognised as 'excellent' and had enhanced antioxidant activity. CONCLUSIONS: Insoluble triticale fibre could therefore be used as a supplement to produce functional yoghurt.
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties
VL  - 98
IS  - 4
SP  - 1291
EP  - 1299
DO  - 10.1002/jsfa.8592
ER  - 

@article{
author = "Miocinovic, Jelena and Tomic, Nikola and Dojnov, Biljana and Tomasević, Igor and Stojanović, Sanja and Đekić, Ilija and Vujčić, Zoran",
year = "2018",
abstract = "BACKGROUND: The need to increase the daily intake of dietary fibres opens a new chapter in the research of functional foods enriched with fibres. The potential application of an innovative product - insoluble dietary fibres from triticale in yoghurts - was deployed by characterising their food application and evaluating physico-chemical, rheological and sensory properties and was the aim of this research. RESULTS: Detailed characterisations of these fibres are presented for the first time and showed very good hydration properties, optimal pH ( slightly acidic), optimal chemical composition, high antioxidant capacity which was proven by phenolics contents. Besides, these fibres showed negligible calorific value, with no phytates and high antioxidant capacity, mainly from ferulic acid. Therefore they could be successfully added to yoghurt. Enrichment of yoghurt having different milk fat content (1.5 and 2.8% w/w) with triticale insoluble fibre (1.5% and 3.0% w/w) significantly influenced the syneresis level, its apparent viscosity, yield stress and thixotropic behaviour. The overall sensory quality scores indicated that yoghurt enriched with 1.5% triticale insoluble fibres was recognised as 'excellent' and had enhanced antioxidant activity. CONCLUSIONS: Insoluble triticale fibre could therefore be used as a supplement to produce functional yoghurt.",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties",
volume = "98",
number = "4",
pages = "1291-1299",
doi = "10.1002/jsfa.8592"
}

Miocinovic, J., Tomic, N., Dojnov, B., Tomasević, I., Stojanović, S., Đekić, I.,& Vujčić, Z.. (2018). Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 98(4), 1291-1299.
https://doi.org/10.1002/jsfa.8592

Miocinovic J, Tomic N, Dojnov B, Tomasević I, Stojanović S, Đekić I, Vujčić Z. Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties. in Journal of the Science of Food and Agriculture. 2018;98(4):1291-1299.
doi:10.1002/jsfa.8592 .

Miocinovic, Jelena, Tomic, Nikola, Dojnov, Biljana, Tomasević, Igor, Stojanović, Sanja, Đekić, Ilija, Vujčić, Zoran, "Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties" in Journal of the Science of Food and Agriculture, 98, no. 4 (2018):1291-1299,
https://doi.org/10.1002/jsfa.8592 . .

TY  - THES
AU  - Jožef, Barbara S.
PY  - 2018
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7670
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22847/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23745033
UR  - https://nardus.mpn.gov.rs/handle/123456789/17609
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3740
AB  - Intenzivan industrijski razvoj propraćen je sve većom kompleksnošću sastava otpadnihvoda. Sintetičke boje su danas u širokoj primeni u velikom broju industrijskih grana. Većinaboja poseduje kompleksnu hemijsku strukturu, kao i povećanu hemijsku stabilnost što ih nakonotpuštanja u vodotokove čini ksenobioticima koji najčešće ispoljavaju i svoje rekalcitrantneosobine. Potreba za novim tehnološkim rešenjima radi uklanjanja širokog spektra ovihobojenih ksenobiotika dovela je do opsežnog istraživanja na ovom polju, dok je u poslednjihnekoliko godina istraživanje na polju primene enzima veoma uznapredovalo.Ova disertacija se bavi izolovanjem kiselih i baznih izoformi peroksidaze iz rena injihovom primenom u uklanjanju različitih obojenih ksenobiotika, optimizacijom reakcijeobezbojavanja, praćenjem i analizom proizvoda zaostalih nakon enzimske degradacije,sintezom imobilizata sa povećanom stabilnošću i efikasnošću u uklanjanju širokog spektraobojenih ksenobiotika. Cilj je bio razvijanje efikasne metode za uklanjanje i detoksifikacijuotpadne vode zaostale nakon procesa bojenja.Izolovanje i prečišćavanje kiselih, baznih i neutralnih izoformi peroksidaze iz renaurađeno je jonoizmenjivačkom hromatografijom na QAE-Sephadex koloni. Razdvojeneizoforme detektovane su zimogramskom detekcijom, nakon izoelektričnog fokusiranja.Optimizovani su uslovi reakcije obezbojavanja primenom rastvornih enzimskih preparata (0,14U mL-1 enzima i 0,44 mM vodonik-peroksida). Testirano je obezbojavanje 24 boje različitihstruktura i karakteristika u zavisnosti od pH i izoforme peroksidaze iz rena. Najveći stepenobezbojavanja postignut je u slučaju 17 boja sa primenom kisele izoforme peroksidaze iz rena:šest pripada klasi azo boja, tri boje triarilmetanskoj i jedna boja tiazinskoj klasi boja dok supreostalih 7 zaštićenih struktura nedostupnih za javnost. U slučaju 12 boja najboljeobezbojavanje postignuto je na pH 5, a u slučaju 10 boja na pH 9. Obezbojavanje je praćenoUV-Vis spektrofotometrijom, a degradacija je potvrđena analizom na HPLC-u.Obezbojavanjem model-boje (оranž II) kiselom izoformom peroksidaze iz rena dobijeniglavnih proizvodi obezbojavanja identifikovani su LC–ESI-ToF-MS tehnikom.Kisela izoforma peroksidaze iz rena uspešno je imobilizovana na 10 komercijalnodostupnih i laboratorijski sintetisanih nosača primenom različitih imobilizacionih tehnika.Kisela izoforma peroksidaze iz rena imobilizovana na hitozanu pokazala je najveću specifičnugvajakolnu aktivnost (2080 U g-1) kao i dekolorizacionu aktivnost uklanjanjem 175 mg L-1model boje. Dobijeni imobilizat pokazao je veću stabilnost prema vodonik-peroksidu upoređenju sa slobodnim enzimom. Imobilizat je pokazao i dobru operativnu stabilnost pa senjegova dekolorizaciona aktivnost nakon 7 ponovljenih ciklusa smanjila za samo 35%.Procena toksičnosti boja i proizvoda obezbojavanja ispitana je na Artemia salina.Obezbojavanje model-boja dovelo je do smanjenja % mortaliteta larvi A. salina u odnosu napočetni rastvor. Ekogenotoksičnost 8 model-boja testirana je na BEAS-2B ćelijama osnovnimi modifikovanim komet testom. Detektovani stepen oštećenja DNA iznosio je od 5 do 47%. Uslučaju model-boje, oranž II detektovana su oksidativna oštećenja pri izlaganju ćelija rastvoruboje (300 μg mL-1), dok izlaganje proizvodima degradacije nakon enzimskog tretmana sakiselom izoformom peroksidaze iz rena ne dovodi do istog efekta.Ispitane su interakcije boja i proizvoda degradacije sa DNA iz telećeg timusa iplazmidnom DNA na model boji oranž II i amido crno 10b primenom UV–Vis i fluorescentnespektrometrije i agaroznom elektroforezom. Nije uočeno značajno cepanje plazmidnogmolekula DNA nakon izlaganja rastvorima boja pre i nakon enzimskog obezbojavanja.
AB  - Intense industrial development has been accompanied by higher complexity ofeffluents. Synthetic dyes have been widely used in great number of industrial sectors.Majority of dyes possesses complex chemical structures, as well as chemical stability,which makes them persistent xenobiotics after their release in water bodies. The need fornew technological solutions for removal of these colored xenobiotics has led to majorongoing research on this field with big emphasis on enzyme application.Subject of this doctoral dissertation is isolation and application of acidic and basichorseradish peroxidase isoforms in decolorization of various colored xenobiotics,optimization of decolorization reactions, monitoring and analysis of decolorizationproducts, synthesis of immobilizates with higher stability and efficiency in removal ofwide spectrum of colored xenobiotics in order to develop efficient method for removaland detoxification of wastewater after the coloring process.Acidic isoforms have been purified from basic and neutral horseradish isoformsusing ion exchange chromatography on QAE-Sephadex column. Separated isoformshave been detected by zymograms after the isoelectric focusing. Decolorization reactionhas been optimized using soluble enzyme isoforms (0.14 U mL-1 and 0.44 mM hydrogenperoxide). Decolorization of 24 dyes of various structures and characteristics have beentested depending of pH and peroxidase isoforms. In case of 17 dyes highestdecolorization has been achieved using acidic horseradish peroxidase: six dyes are fromazo, three from triarylmethane and one from thiazine category while the rest of dyes havestructure which is unavailable to the public. Twelve dyes were decolorized best at pH 5,while 10 dyes were decolorized best at pH 9. Decolorization was monitored by UV–Visspectrometry, while degradation was confirmed by HPLC. By decolorization of modeldye (orange II) using acidic horseradish peroxidase the main decolorization productswere identified by LC–ESI-ToF-MS technique.Acidic isoform has been successfully immobilized on 10 commercially availableand laboratory synthetized carriers by various immobilization techniques. Acidichorseradish isoform immobilized on chitosan has shown highest specific activity towardguaiacol (2080 U g-1) as well as decolorization acvitity by removal of 175 mg L-1 ofmodel dye. The immobilizate obtained showed higher stability towards hydrogenperoxide in comparison with the soluble enzyme. The immobilizate has shown goodoperative stability since it has retained 65% of its decolorization activity after 7 repeatedcycles. The assessment of toxicity of dyes and decolorization products has been testedon Artemia salina. Decolorization of model dye has resulted in reduction of mortality ofA. salina larvae in comparison with initial dye. Ecogenotoxcitiy of 8 model dyes has beentested on BEAS-2B cells using basic and modified comet assay. DNA damage detectedwas from 5 to 47%. In case of model dye, orange II, oxidative DNA damage has beendetected after the exposure of cells to dye solutions (300 μg mL-1), while degradationproducts after enzymatic decolorization with acidic horseradish peroxidase showed noDNA damage.Interactions of dyes and degradation products with DNA from calf thymus andplasmid DNA has been studied using model dye orange II and amido black 10b by UV–Vis and fluorescent spectroscopy and agarose electrophoresis. Significant DNA strandbreaks on plasmid DNA has not been detected in either case.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Primena rastvornih i imobilizovanih izoformi peroksidaze iz rena u uklanjanju obojenih ksenobiotika iz otpadne vode
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17609
ER  - 

@phdthesis{
author = "Jožef, Barbara S.",
year = "2018",
abstract = "Intenzivan industrijski razvoj propraćen je sve većom kompleksnošću sastava otpadnihvoda. Sintetičke boje su danas u širokoj primeni u velikom broju industrijskih grana. Većinaboja poseduje kompleksnu hemijsku strukturu, kao i povećanu hemijsku stabilnost što ih nakonotpuštanja u vodotokove čini ksenobioticima koji najčešće ispoljavaju i svoje rekalcitrantneosobine. Potreba za novim tehnološkim rešenjima radi uklanjanja širokog spektra ovihobojenih ksenobiotika dovela je do opsežnog istraživanja na ovom polju, dok je u poslednjihnekoliko godina istraživanje na polju primene enzima veoma uznapredovalo.Ova disertacija se bavi izolovanjem kiselih i baznih izoformi peroksidaze iz rena injihovom primenom u uklanjanju različitih obojenih ksenobiotika, optimizacijom reakcijeobezbojavanja, praćenjem i analizom proizvoda zaostalih nakon enzimske degradacije,sintezom imobilizata sa povećanom stabilnošću i efikasnošću u uklanjanju širokog spektraobojenih ksenobiotika. Cilj je bio razvijanje efikasne metode za uklanjanje i detoksifikacijuotpadne vode zaostale nakon procesa bojenja.Izolovanje i prečišćavanje kiselih, baznih i neutralnih izoformi peroksidaze iz renaurađeno je jonoizmenjivačkom hromatografijom na QAE-Sephadex koloni. Razdvojeneizoforme detektovane su zimogramskom detekcijom, nakon izoelektričnog fokusiranja.Optimizovani su uslovi reakcije obezbojavanja primenom rastvornih enzimskih preparata (0,14U mL-1 enzima i 0,44 mM vodonik-peroksida). Testirano je obezbojavanje 24 boje različitihstruktura i karakteristika u zavisnosti od pH i izoforme peroksidaze iz rena. Najveći stepenobezbojavanja postignut je u slučaju 17 boja sa primenom kisele izoforme peroksidaze iz rena:šest pripada klasi azo boja, tri boje triarilmetanskoj i jedna boja tiazinskoj klasi boja dok supreostalih 7 zaštićenih struktura nedostupnih za javnost. U slučaju 12 boja najboljeobezbojavanje postignuto je na pH 5, a u slučaju 10 boja na pH 9. Obezbojavanje je praćenoUV-Vis spektrofotometrijom, a degradacija je potvrđena analizom na HPLC-u.Obezbojavanjem model-boje (оranž II) kiselom izoformom peroksidaze iz rena dobijeniglavnih proizvodi obezbojavanja identifikovani su LC–ESI-ToF-MS tehnikom.Kisela izoforma peroksidaze iz rena uspešno je imobilizovana na 10 komercijalnodostupnih i laboratorijski sintetisanih nosača primenom različitih imobilizacionih tehnika.Kisela izoforma peroksidaze iz rena imobilizovana na hitozanu pokazala je najveću specifičnugvajakolnu aktivnost (2080 U g-1) kao i dekolorizacionu aktivnost uklanjanjem 175 mg L-1model boje. Dobijeni imobilizat pokazao je veću stabilnost prema vodonik-peroksidu upoređenju sa slobodnim enzimom. Imobilizat je pokazao i dobru operativnu stabilnost pa senjegova dekolorizaciona aktivnost nakon 7 ponovljenih ciklusa smanjila za samo 35%.Procena toksičnosti boja i proizvoda obezbojavanja ispitana je na Artemia salina.Obezbojavanje model-boja dovelo je do smanjenja % mortaliteta larvi A. salina u odnosu napočetni rastvor. Ekogenotoksičnost 8 model-boja testirana je na BEAS-2B ćelijama osnovnimi modifikovanim komet testom. Detektovani stepen oštećenja DNA iznosio je od 5 do 47%. Uslučaju model-boje, oranž II detektovana su oksidativna oštećenja pri izlaganju ćelija rastvoruboje (300 μg mL-1), dok izlaganje proizvodima degradacije nakon enzimskog tretmana sakiselom izoformom peroksidaze iz rena ne dovodi do istog efekta.Ispitane su interakcije boja i proizvoda degradacije sa DNA iz telećeg timusa iplazmidnom DNA na model boji oranž II i amido crno 10b primenom UV–Vis i fluorescentnespektrometrije i agaroznom elektroforezom. Nije uočeno značajno cepanje plazmidnogmolekula DNA nakon izlaganja rastvorima boja pre i nakon enzimskog obezbojavanja., Intense industrial development has been accompanied by higher complexity ofeffluents. Synthetic dyes have been widely used in great number of industrial sectors.Majority of dyes possesses complex chemical structures, as well as chemical stability,which makes them persistent xenobiotics after their release in water bodies. The need fornew technological solutions for removal of these colored xenobiotics has led to majorongoing research on this field with big emphasis on enzyme application.Subject of this doctoral dissertation is isolation and application of acidic and basichorseradish peroxidase isoforms in decolorization of various colored xenobiotics,optimization of decolorization reactions, monitoring and analysis of decolorizationproducts, synthesis of immobilizates with higher stability and efficiency in removal ofwide spectrum of colored xenobiotics in order to develop efficient method for removaland detoxification of wastewater after the coloring process.Acidic isoforms have been purified from basic and neutral horseradish isoformsusing ion exchange chromatography on QAE-Sephadex column. Separated isoformshave been detected by zymograms after the isoelectric focusing. Decolorization reactionhas been optimized using soluble enzyme isoforms (0.14 U mL-1 and 0.44 mM hydrogenperoxide). Decolorization of 24 dyes of various structures and characteristics have beentested depending of pH and peroxidase isoforms. In case of 17 dyes highestdecolorization has been achieved using acidic horseradish peroxidase: six dyes are fromazo, three from triarylmethane and one from thiazine category while the rest of dyes havestructure which is unavailable to the public. Twelve dyes were decolorized best at pH 5,while 10 dyes were decolorized best at pH 9. Decolorization was monitored by UV–Visspectrometry, while degradation was confirmed by HPLC. By decolorization of modeldye (orange II) using acidic horseradish peroxidase the main decolorization productswere identified by LC–ESI-ToF-MS technique.Acidic isoform has been successfully immobilized on 10 commercially availableand laboratory synthetized carriers by various immobilization techniques. Acidichorseradish isoform immobilized on chitosan has shown highest specific activity towardguaiacol (2080 U g-1) as well as decolorization acvitity by removal of 175 mg L-1 ofmodel dye. The immobilizate obtained showed higher stability towards hydrogenperoxide in comparison with the soluble enzyme. The immobilizate has shown goodoperative stability since it has retained 65% of its decolorization activity after 7 repeatedcycles. The assessment of toxicity of dyes and decolorization products has been testedon Artemia salina. Decolorization of model dye has resulted in reduction of mortality ofA. salina larvae in comparison with initial dye. Ecogenotoxcitiy of 8 model dyes has beentested on BEAS-2B cells using basic and modified comet assay. DNA damage detectedwas from 5 to 47%. In case of model dye, orange II, oxidative DNA damage has beendetected after the exposure of cells to dye solutions (300 μg mL-1), while degradationproducts after enzymatic decolorization with acidic horseradish peroxidase showed noDNA damage.Interactions of dyes and degradation products with DNA from calf thymus andplasmid DNA has been studied using model dye orange II and amido black 10b by UV–Vis and fluorescent spectroscopy and agarose electrophoresis. Significant DNA strandbreaks on plasmid DNA has not been detected in either case.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Primena rastvornih i imobilizovanih izoformi peroksidaze iz rena u uklanjanju obojenih ksenobiotika iz otpadne vode",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17609"
}

Jožef, B. S.. (2018). Primena rastvornih i imobilizovanih izoformi peroksidaze iz rena u uklanjanju obojenih ksenobiotika iz otpadne vode. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17609

Jožef BS. Primena rastvornih i imobilizovanih izoformi peroksidaze iz rena u uklanjanju obojenih ksenobiotika iz otpadne vode. in Универзитет у Београду. 2018;.
https://hdl.handle.net/21.15107/rcub_nardus_17609 .

Jožef, Barbara S., "Primena rastvornih i imobilizovanih izoformi peroksidaze iz rena u uklanjanju obojenih ksenobiotika iz otpadne vode" in Универзитет у Београду (2018),
https://hdl.handle.net/21.15107/rcub_nardus_17609 .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Josić, Djuro
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2287
AB  - Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.
PB  - Elsevier Science London, London
T2  - Trends in Food Science & Technology
T1  - Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety
VL  - 77
SP  - 100
EP  - 119
DO  - 10.1016/j.tifs.2018.04.008
ER  - 

@article{
author = "Anđelković, Uroš and Josić, Djuro",
year = "2018",
abstract = "Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.",
publisher = "Elsevier Science London, London",
journal = "Trends in Food Science & Technology",
title = "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety",
volume = "77",
pages = "100-119",
doi = "10.1016/j.tifs.2018.04.008"
}

Anđelković, U.,& Josić, D.. (2018). Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology
Elsevier Science London, London., 77, 100-119.
https://doi.org/10.1016/j.tifs.2018.04.008

Anđelković U, Josić D. Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology. 2018;77:100-119.
doi:10.1016/j.tifs.2018.04.008 .

Anđelković, Uroš, Josić, Djuro, "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety" in Trends in Food Science & Technology, 77 (2018):100-119,
https://doi.org/10.1016/j.tifs.2018.04.008 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Josić, Djuro
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4280
AB  - Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.
PB  - Elsevier Science London, London
T2  - Trends in Food Science & Technology
T1  - Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety
VL  - 77
SP  - 100
EP  - 119
DO  - 10.1016/j.tifs.2018.04.008
ER  - 

@article{
author = "Anđelković, Uroš and Josić, Djuro",
year = "2018",
abstract = "Background.: As a comprehensive discipline that studies food and nutrition, foodomics requires reliable qualitative and quantitative information about the food proteome component in order to extract new integrative information from the complex multivariable space of omics. This new information is necessary to achieve a higher level of understanding of processes in food science and technology, consequently new functions of food and improved markers of food quality and safety and completely transform concept of food safety. Scope and approach: We are making an effort to present mass spectrometry (MS) based proteomic approaches that are being utilized in different proteomic studies, not necessarily in the field of foodomics, which are important and have the potential to advance this field. Current analytical capabilities of MS-based proteomics together with sample preparation procedures and quantification strategies, and recent technical developments were presented. Key findings and conclusions: MS-based proteomics enables the analysis of different aspects of proteins and provides a variety of approaches for reliable quantification of individual proteinsand/or food proteome. This is a complex field and its successful implementation requires a dedicated analyst, a thorough design of sample preparation procedure, the selection of an MS technique and approach, an adequate type of mass spectrometer, a thorough data analysis and validation. Improvements in the technology of mass spectrometers are continuously expanding capabilities of MS-based proteomics.",
publisher = "Elsevier Science London, London",
journal = "Trends in Food Science & Technology",
title = "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety",
volume = "77",
pages = "100-119",
doi = "10.1016/j.tifs.2018.04.008"
}

Anđelković, U.,& Josić, D.. (2018). Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology
Elsevier Science London, London., 77, 100-119.
https://doi.org/10.1016/j.tifs.2018.04.008

Anđelković U, Josić D. Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety. in Trends in Food Science & Technology. 2018;77:100-119.
doi:10.1016/j.tifs.2018.04.008 .

Anđelković, Uroš, Josić, Djuro, "Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety" in Trends in Food Science & Technology, 77 (2018):100-119,
https://doi.org/10.1016/j.tifs.2018.04.008 . .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2185
AB  - Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Preparative Biochemistry & Biotechnology
T1  - Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae
VL  - 47
IS  - 3
SP  - 305
EP  - 311
DO  - 10.1080/10826068.2016.1244683
ER  - 

@article{
author = "Margetić, Aleksandra and Vujčić, Zoran",
year = "2017",
abstract = "Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Preparative Biochemistry & Biotechnology",
title = "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae",
volume = "47",
number = "3",
pages = "305-311",
doi = "10.1080/10826068.2016.1244683"
}

Margetić, A.,& Vujčić, Z.. (2017). Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry & Biotechnology
Taylor & Francis Inc, Philadelphia., 47(3), 305-311.
https://doi.org/10.1080/10826068.2016.1244683

Margetić A, Vujčić Z. Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry & Biotechnology. 2017;47(3):305-311.
doi:10.1080/10826068.2016.1244683 .

Margetić, Aleksandra, Vujčić, Zoran, "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae" in Preparative Biochemistry & Biotechnology, 47, no. 3 (2017):305-311,
https://doi.org/10.1080/10826068.2016.1244683 . .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3066
AB  - Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Preparative Biochemistry & Biotechnology
T1  - Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae
VL  - 47
IS  - 3
SP  - 305
EP  - 311
DO  - 10.1080/10826068.2016.1244683
ER  - 

@article{
author = "Margetić, Aleksandra and Vujčić, Zoran",
year = "2017",
abstract = "Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Preparative Biochemistry & Biotechnology",
title = "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae",
volume = "47",
number = "3",
pages = "305-311",
doi = "10.1080/10826068.2016.1244683"
}

Margetić, A.,& Vujčić, Z.. (2017). Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry & Biotechnology
Taylor & Francis Inc, Philadelphia., 47(3), 305-311.
https://doi.org/10.1080/10826068.2016.1244683

Margetić A, Vujčić Z. Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry & Biotechnology. 2017;47(3):305-311.
doi:10.1080/10826068.2016.1244683 .

Margetić, Aleksandra, Vujčić, Zoran, "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae" in Preparative Biochemistry & Biotechnology, 47, no. 3 (2017):305-311,
https://doi.org/10.1080/10826068.2016.1244683 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinović, Tamara
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2113
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier Sci Ltd, Oxford
T2  - Trac-Trends in Analytical Chemistry
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinović, Tamara and Josić, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Trac-Trends in Analytical Chemistry",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinović, T.,& Josić, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry
Elsevier Sci Ltd, Oxford., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinović T, Josić D. Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinović, Tamara, Josić, Djuro, "Omics methods as a tool for investigation of food allergies" in Trac-Trends in Analytical Chemistry, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinović, Tamara
AU  - Josić, Djuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2937
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier
T2  - Trac-Trends in Analytical Chemistry
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinović, Tamara and Josić, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier",
journal = "Trac-Trends in Analytical Chemistry",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinović, T.,& Josić, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry
Elsevier., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinović T, Josić D. Omics methods as a tool for investigation of food allergies. in Trac-Trends in Analytical Chemistry. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinović, Tamara, Josić, Djuro, "Omics methods as a tool for investigation of food allergies" in Trac-Trends in Analytical Chemistry, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Miocinovic, Jelena
AU  - Tomasević, Igor
AU  - Smigic, Nada
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2258
AB  - Fortification of fermented dairy products with insoluble dietary fiber is an interesting way to increase consumers' fiber intake. The objective of this study was to evaluate the sensory characteristics and consumer acceptance of low-fat unsweetened yoghurt, fortified at levels of 15 and 30 g/kg, with insoluble triticale, wheat or oat fibers. The addition of insoluble triticale fiber resulted in yellowish-brown color, grainy flavor, and pronounced sandiness/grittiness of the fortified yoghurts. The products were classified into the 'very good' quality category, despite the lower quality scores given to the 30 g/kg fiber fortified yoghurts, caused primarily by a gritty/sandy texture and some bitterness. Three distinct consumer subgroups were revealed by the clustering analysis, one of which showed a preference for the triticale-yoghurts. Insoluble dietary fiber from triticale showed promising potential to be used as a fortifying ingredient in the production of fiber-enriched fermented dairy products such as yoghurt.
PB  - Elsevier
T2  - Lwt-Food Science and Technology
T1  - Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective
VL  - 80
SP  - 59
EP  - 66
DO  - 10.1016/j.lwt.2017.02.008
ER  - 

@article{
author = "Tomić, Nikola and Dojnov, Biljana and Miocinovic, Jelena and Tomasević, Igor and Smigic, Nada and Đekić, Ilija and Vujčić, Zoran",
year = "2017",
abstract = "Fortification of fermented dairy products with insoluble dietary fiber is an interesting way to increase consumers' fiber intake. The objective of this study was to evaluate the sensory characteristics and consumer acceptance of low-fat unsweetened yoghurt, fortified at levels of 15 and 30 g/kg, with insoluble triticale, wheat or oat fibers. The addition of insoluble triticale fiber resulted in yellowish-brown color, grainy flavor, and pronounced sandiness/grittiness of the fortified yoghurts. The products were classified into the 'very good' quality category, despite the lower quality scores given to the 30 g/kg fiber fortified yoghurts, caused primarily by a gritty/sandy texture and some bitterness. Three distinct consumer subgroups were revealed by the clustering analysis, one of which showed a preference for the triticale-yoghurts. Insoluble dietary fiber from triticale showed promising potential to be used as a fortifying ingredient in the production of fiber-enriched fermented dairy products such as yoghurt.",
publisher = "Elsevier",
journal = "Lwt-Food Science and Technology",
title = "Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective",
volume = "80",
pages = "59-66",
doi = "10.1016/j.lwt.2017.02.008"
}

Tomić, N., Dojnov, B., Miocinovic, J., Tomasević, I., Smigic, N., Đekić, I.,& Vujčić, Z.. (2017). Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective. in Lwt-Food Science and Technology
Elsevier., 80, 59-66.
https://doi.org/10.1016/j.lwt.2017.02.008

Tomić N, Dojnov B, Miocinovic J, Tomasević I, Smigic N, Đekić I, Vujčić Z. Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective. in Lwt-Food Science and Technology. 2017;80:59-66.
doi:10.1016/j.lwt.2017.02.008 .

Tomić, Nikola, Dojnov, Biljana, Miocinovic, Jelena, Tomasević, Igor, Smigic, Nada, Đekić, Ilija, Vujčić, Zoran, "Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective" in Lwt-Food Science and Technology, 80 (2017):59-66,
https://doi.org/10.1016/j.lwt.2017.02.008 . .

TY  - JOUR
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Miocinovic, Jelena
AU  - Tomasević, Igor
AU  - Smigic, Nada
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2981
AB  - Fortification of fermented dairy products with insoluble dietary fiber is an interesting way to increase consumers' fiber intake. The objective of this study was to evaluate the sensory characteristics and consumer acceptance of low-fat unsweetened yoghurt, fortified at levels of 15 and 30 g/kg, with insoluble triticale, wheat or oat fibers. The addition of insoluble triticale fiber resulted in yellowish-brown color, grainy flavor, and pronounced sandiness/grittiness of the fortified yoghurts. The products were classified into the 'very good' quality category, despite the lower quality scores given to the 30 g/kg fiber fortified yoghurts, caused primarily by a gritty/sandy texture and some bitterness. Three distinct consumer subgroups were revealed by the clustering analysis, one of which showed a preference for the triticale-yoghurts. Insoluble dietary fiber from triticale showed promising potential to be used as a fortifying ingredient in the production of fiber-enriched fermented dairy products such as yoghurt.
PB  - Elsevier
T2  - Lwt-Food Science and Technology
T1  - Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective
VL  - 80
SP  - 59
EP  - 66
DO  - 10.1016/j.lwt.2017.02.008
ER  - 

@article{
author = "Tomić, Nikola and Dojnov, Biljana and Miocinovic, Jelena and Tomasević, Igor and Smigic, Nada and Đekić, Ilija and Vujčić, Zoran",
year = "2017",
abstract = "Fortification of fermented dairy products with insoluble dietary fiber is an interesting way to increase consumers' fiber intake. The objective of this study was to evaluate the sensory characteristics and consumer acceptance of low-fat unsweetened yoghurt, fortified at levels of 15 and 30 g/kg, with insoluble triticale, wheat or oat fibers. The addition of insoluble triticale fiber resulted in yellowish-brown color, grainy flavor, and pronounced sandiness/grittiness of the fortified yoghurts. The products were classified into the 'very good' quality category, despite the lower quality scores given to the 30 g/kg fiber fortified yoghurts, caused primarily by a gritty/sandy texture and some bitterness. Three distinct consumer subgroups were revealed by the clustering analysis, one of which showed a preference for the triticale-yoghurts. Insoluble dietary fiber from triticale showed promising potential to be used as a fortifying ingredient in the production of fiber-enriched fermented dairy products such as yoghurt.",
publisher = "Elsevier",
journal = "Lwt-Food Science and Technology",
title = "Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective",
volume = "80",
pages = "59-66",
doi = "10.1016/j.lwt.2017.02.008"
}

Tomić, N., Dojnov, B., Miocinovic, J., Tomasević, I., Smigic, N., Đekić, I.,& Vujčić, Z.. (2017). Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective. in Lwt-Food Science and Technology
Elsevier., 80, 59-66.
https://doi.org/10.1016/j.lwt.2017.02.008

Tomić N, Dojnov B, Miocinovic J, Tomasević I, Smigic N, Đekić I, Vujčić Z. Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective. in Lwt-Food Science and Technology. 2017;80:59-66.
doi:10.1016/j.lwt.2017.02.008 .

Tomić, Nikola, Dojnov, Biljana, Miocinovic, Jelena, Tomasević, Igor, Smigic, Nada, Đekić, Ilija, Vujčić, Zoran, "Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective" in Lwt-Food Science and Technology, 80 (2017):59-66,
https://doi.org/10.1016/j.lwt.2017.02.008 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2122
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Šrajer Gajdošik, Martina
AU  - Gašo-Sokač, Dajana
AU  - Martinović, Tamara
AU  - Josić, Đuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2156
AB  - The power of foodomics as a discipline that is now broadly used for quality assurance of food products and adulteration identifi cation, as well as for determining the safety of food, is presented. Concerning sample preparation and application, maintenance of highly sophisticated instruments for both high-performance and high-throughput techniques, and analysis and data interpretation, special att ention has to be paid to the development of skilled analysts. The obtained data shall be integrated under a strong bioinformatics environment. Modern mass spectrometry is an extremely powerful analytical tool since it can provide direct qualitative and quantitative information about a molecule of interest from only a minute amount of sample. Quality of this information is infl uenced by the sample preparation procedure, the type of mass spectrometer used and the analyst's skills. Technical advances are bringing new instruments of increased sensitivity, resolution and speed to the market. Other methods presented here give additional information and can be used as complementary tools to mass spectrometry or for validation of obtained results. Genomics and transcriptomics, as well as affi nity-based methods, still have a broad use in food analysis. Serious drawbacks of some of them, especially the affi nity-based methods, are the cross-reactivity between similar molecules and the infl uence of complex food matrices. However, these techniques can be used for pre-screening in order to reduce the large number of samples. Great progress has been made in the application of bioinformatics in foodomics. These developments enabled processing of large amounts of generated data for both identifi cation and quantifi cation, and for corresponding modeling.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Foodomics and Food Safety: Where We Are
VL  - 55
IS  - 3
SP  - 290
EP  - 307
DO  - 10.17113/ftb.55.03.17.5044
ER  - 

@article{
author = "Anđelković, Uroš and Šrajer Gajdošik, Martina and Gašo-Sokač, Dajana and Martinović, Tamara and Josić, Đuro",
year = "2017",
abstract = "The power of foodomics as a discipline that is now broadly used for quality assurance of food products and adulteration identifi cation, as well as for determining the safety of food, is presented. Concerning sample preparation and application, maintenance of highly sophisticated instruments for both high-performance and high-throughput techniques, and analysis and data interpretation, special att ention has to be paid to the development of skilled analysts. The obtained data shall be integrated under a strong bioinformatics environment. Modern mass spectrometry is an extremely powerful analytical tool since it can provide direct qualitative and quantitative information about a molecule of interest from only a minute amount of sample. Quality of this information is infl uenced by the sample preparation procedure, the type of mass spectrometer used and the analyst's skills. Technical advances are bringing new instruments of increased sensitivity, resolution and speed to the market. Other methods presented here give additional information and can be used as complementary tools to mass spectrometry or for validation of obtained results. Genomics and transcriptomics, as well as affi nity-based methods, still have a broad use in food analysis. Serious drawbacks of some of them, especially the affi nity-based methods, are the cross-reactivity between similar molecules and the infl uence of complex food matrices. However, these techniques can be used for pre-screening in order to reduce the large number of samples. Great progress has been made in the application of bioinformatics in foodomics. These developments enabled processing of large amounts of generated data for both identifi cation and quantifi cation, and for corresponding modeling.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Foodomics and Food Safety: Where We Are",
volume = "55",
number = "3",
pages = "290-307",
doi = "10.17113/ftb.55.03.17.5044"
}

Anđelković, U., Šrajer Gajdošik, M., Gašo-Sokač, D., Martinović, T.,& Josić, Đ.. (2017). Foodomics and Food Safety: Where We Are. in Food Technology and Biotechnology
University of Zagreb., 55(3), 290-307.
https://doi.org/10.17113/ftb.55.03.17.5044

Anđelković U, Šrajer Gajdošik M, Gašo-Sokač D, Martinović T, Josić Đ. Foodomics and Food Safety: Where We Are. in Food Technology and Biotechnology. 2017;55(3):290-307.
doi:10.17113/ftb.55.03.17.5044 .

Anđelković, Uroš, Šrajer Gajdošik, Martina, Gašo-Sokač, Dajana, Martinović, Tamara, Josić, Đuro, "Foodomics and Food Safety: Where We Are" in Food Technology and Biotechnology, 55, no. 3 (2017):290-307,
https://doi.org/10.17113/ftb.55.03.17.5044 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2985
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700260
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700260"
}

Anđelković, U., Tufegdžić, S.,& Popović, M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700260

Anđelković U, Tufegdžić S, Popović M. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700260 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica, "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700260 . .

TY  - CHAP
AU  - Anđelković, Uroš
AU  - Giacometti, Jasminka
AU  - Josić, Đuro
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4233
AB  - Since the introduction of suitable, highly porous supports and later nonporous and monolithic supports, chromatography has been an indispensibleindispensable method for protein separations on the analytical and preparative scales. The most frequently used methods for protein chromatography are ion exchange, reversed- phase, hydrophobic hydrophobic-interaction chromatography, chromatography on hydroxyapatite and different types of affinity, and pseudo-affinity chromatography. Because of the use of organic solvents during the separation in reversed-phase chromatography, denaturation and loss of biological activity frequently occurs, and this method is less suitable for the separation of biologically active, therapeutic proteins. Chromatography on monolithic supports and chromatography in the displacement mode offer additional opportunities for fast, highly effective separation of proteins on both the analytical and preparative scales.
PB  - Elsevier
T2  - Liquid Chromatography: Applications
T1  - Protein and Peptide Separations
VL  - 2
SP  - 107
EP  - 157
DO  - 10.1016/B978-0-12-805392-8.00005-0
ER  - 

@inbook{
author = "Anđelković, Uroš and Giacometti, Jasminka and Josić, Đuro",
year = "2017",
abstract = "Since the introduction of suitable, highly porous supports and later nonporous and monolithic supports, chromatography has been an indispensibleindispensable method for protein separations on the analytical and preparative scales. The most frequently used methods for protein chromatography are ion exchange, reversed- phase, hydrophobic hydrophobic-interaction chromatography, chromatography on hydroxyapatite and different types of affinity, and pseudo-affinity chromatography. Because of the use of organic solvents during the separation in reversed-phase chromatography, denaturation and loss of biological activity frequently occurs, and this method is less suitable for the separation of biologically active, therapeutic proteins. Chromatography on monolithic supports and chromatography in the displacement mode offer additional opportunities for fast, highly effective separation of proteins on both the analytical and preparative scales.",
publisher = "Elsevier",
journal = "Liquid Chromatography: Applications",
booktitle = "Protein and Peptide Separations",
volume = "2",
pages = "107-157",
doi = "10.1016/B978-0-12-805392-8.00005-0"
}

Anđelković, U., Giacometti, J.,& Josić, Đ.. (2017). Protein and Peptide Separations. in Liquid Chromatography: Applications
Elsevier., 2, 107-157.
https://doi.org/10.1016/B978-0-12-805392-8.00005-0

Anđelković U, Giacometti J, Josić Đ. Protein and Peptide Separations. in Liquid Chromatography: Applications. 2017;2:107-157.
doi:10.1016/B978-0-12-805392-8.00005-0 .

Anđelković, Uroš, Giacometti, Jasminka, Josić, Đuro, "Protein and Peptide Separations" in Liquid Chromatography: Applications, 2 (2017):107-157,
https://doi.org/10.1016/B978-0-12-805392-8.00005-0 . .

TY  - JOUR
AU  - Janović, Barbara
AU  - Collins, Andrew R.
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3045
AB  - The aim of this study was to investigate the impact of dyes on DNA before and after enzymatic decolorization by acidic horseradish peroxidase (HRP-A). The comet assay is easy and feasible method widely used to measure DNA damage and repair. The medium-throughput comet assay was employed for assessment of genotoxic effects of 8 dyes in BEAS-2B cells. We have incorporated a digestion with bacterial endonuclease (formamidopyrimidine DNA glycosylase, FPG) to detect oxidized bases in the case of single and double azo dyes, Orange II (OR2) and Amido Black 10B (AB), respectively. This allowed detection 8-oxo7,8-dihydroguanine, one of most abundant oxidized bases in nuclear DNA. In the case of AB there was no indication of DNA damage, either strand brakes or FPG-sensitive sites before and after decolorization. The OR2 induced DNA damage (in terms of percentage of DNA in comet tails). Also, the frequency of FPG-sensitive sites increased with OR2 concentration. After decolorization no DNA damaging effects was seen at all. The interaction studies of OR2 and AB, before and after decolorization, with calf thymus DNA has been investigated by absorption and fluorescence spectroscopy. The results provide support for the idea that in some cases enzymatic decolorization contributes to lower genotoxicity potential.
PB  - Elsevier
T2  - Journal of Hazardous Materials
T1  - Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes
VL  - 321
SP  - 576
EP  - 585
DO  - 10.1016/j.jhazmat.2016.09.037
ER  - 

@article{
author = "Janović, Barbara and Collins, Andrew R. and Vujčić, Zoran and Vujčić, Miroslava",
year = "2017",
abstract = "The aim of this study was to investigate the impact of dyes on DNA before and after enzymatic decolorization by acidic horseradish peroxidase (HRP-A). The comet assay is easy and feasible method widely used to measure DNA damage and repair. The medium-throughput comet assay was employed for assessment of genotoxic effects of 8 dyes in BEAS-2B cells. We have incorporated a digestion with bacterial endonuclease (formamidopyrimidine DNA glycosylase, FPG) to detect oxidized bases in the case of single and double azo dyes, Orange II (OR2) and Amido Black 10B (AB), respectively. This allowed detection 8-oxo7,8-dihydroguanine, one of most abundant oxidized bases in nuclear DNA. In the case of AB there was no indication of DNA damage, either strand brakes or FPG-sensitive sites before and after decolorization. The OR2 induced DNA damage (in terms of percentage of DNA in comet tails). Also, the frequency of FPG-sensitive sites increased with OR2 concentration. After decolorization no DNA damaging effects was seen at all. The interaction studies of OR2 and AB, before and after decolorization, with calf thymus DNA has been investigated by absorption and fluorescence spectroscopy. The results provide support for the idea that in some cases enzymatic decolorization contributes to lower genotoxicity potential.",
publisher = "Elsevier",
journal = "Journal of Hazardous Materials",
title = "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes",
volume = "321",
pages = "576-585",
doi = "10.1016/j.jhazmat.2016.09.037"
}

Janović, B., Collins, A. R., Vujčić, Z.,& Vujčić, M.. (2017). Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes. in Journal of Hazardous Materials
Elsevier., 321, 576-585.
https://doi.org/10.1016/j.jhazmat.2016.09.037

Janović B, Collins AR, Vujčić Z, Vujčić M. Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes. in Journal of Hazardous Materials. 2017;321:576-585.
doi:10.1016/j.jhazmat.2016.09.037 .

Janović, Barbara, Collins, Andrew R., Vujčić, Zoran, Vujčić, Miroslava, "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes" in Journal of Hazardous Materials, 321 (2017):576-585,
https://doi.org/10.1016/j.jhazmat.2016.09.037 . .

TY  - JOUR
AU  - Janović, Barbara
AU  - Collins, Andrew R.
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2070
AB  - The aim of this study was to investigate the impact of dyes on DNA before and after enzymatic decolorization by acidic horseradish peroxidase (HRP-A). The comet assay is easy and feasible method widely used to measure DNA damage and repair. The medium-throughput comet assay was employed for assessment of genotoxic effects of 8 dyes in BEAS-2B cells. We have incorporated a digestion with bacterial endonuclease (formamidopyrimidine DNA glycosylase, FPG) to detect oxidized bases in the case of single and double azo dyes, Orange II (OR2) and Amido Black 10B (AB), respectively. This allowed detection 8-oxo7,8-dihydroguanine, one of most abundant oxidized bases in nuclear DNA. In the case of AB there was no indication of DNA damage, either strand brakes or FPG-sensitive sites before and after decolorization. The OR2 induced DNA damage (in terms of percentage of DNA in comet tails). Also, the frequency of FPG-sensitive sites increased with OR2 concentration. After decolorization no DNA damaging effects was seen at all. The interaction studies of OR2 and AB, before and after decolorization, with calf thymus DNA has been investigated by absorption and fluorescence spectroscopy. The results provide support for the idea that in some cases enzymatic decolorization contributes to lower genotoxicity potential.
PB  - Elsevier
T2  - Journal of Hazardous Materials
T1  - Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes
VL  - 321
SP  - 576
EP  - 585
DO  - 10.1016/j.jhazmat.2016.09.037
ER  - 

@article{
author = "Janović, Barbara and Collins, Andrew R. and Vujčić, Zoran and Vujčić, Miroslava",
year = "2017",
abstract = "The aim of this study was to investigate the impact of dyes on DNA before and after enzymatic decolorization by acidic horseradish peroxidase (HRP-A). The comet assay is easy and feasible method widely used to measure DNA damage and repair. The medium-throughput comet assay was employed for assessment of genotoxic effects of 8 dyes in BEAS-2B cells. We have incorporated a digestion with bacterial endonuclease (formamidopyrimidine DNA glycosylase, FPG) to detect oxidized bases in the case of single and double azo dyes, Orange II (OR2) and Amido Black 10B (AB), respectively. This allowed detection 8-oxo7,8-dihydroguanine, one of most abundant oxidized bases in nuclear DNA. In the case of AB there was no indication of DNA damage, either strand brakes or FPG-sensitive sites before and after decolorization. The OR2 induced DNA damage (in terms of percentage of DNA in comet tails). Also, the frequency of FPG-sensitive sites increased with OR2 concentration. After decolorization no DNA damaging effects was seen at all. The interaction studies of OR2 and AB, before and after decolorization, with calf thymus DNA has been investigated by absorption and fluorescence spectroscopy. The results provide support for the idea that in some cases enzymatic decolorization contributes to lower genotoxicity potential.",
publisher = "Elsevier",
journal = "Journal of Hazardous Materials",
title = "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes",
volume = "321",
pages = "576-585",
doi = "10.1016/j.jhazmat.2016.09.037"
}

Janović, B., Collins, A. R., Vujčić, Z.,& Vujčić, M.. (2017). Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes. in Journal of Hazardous Materials
Elsevier., 321, 576-585.
https://doi.org/10.1016/j.jhazmat.2016.09.037

Janović B, Collins AR, Vujčić Z, Vujčić M. Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes. in Journal of Hazardous Materials. 2017;321:576-585.
doi:10.1016/j.jhazmat.2016.09.037 .

Janović, Barbara, Collins, Andrew R., Vujčić, Zoran, Vujčić, Miroslava, "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes" in Journal of Hazardous Materials, 321 (2017):576-585,
https://doi.org/10.1016/j.jhazmat.2016.09.037 . .

TY  - JOUR
AU  - Janović, Barbara
AU  - Vicovac, Milica Lj. Micic
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2084
AB  - Peroxidases (EC 1.11.1.7) have enormous biotechnological applications. Usage of more abundant, basic isoforms of peroxidases in diagnostic kits and/or in immunochemistry has led to under exploitation and disregard of horseradish peroxidase (HRP) acidic isoforms. Therefore, acidic horseradish peroxidase (HRP-A) isoenzymewas used for the preparation of a biocatalyst with improved ability in dye decolorization. Ten biocatalysts were prepared by covalent binding of enzyme to chitosan and alginate, adsorption followed by cross-linking on inorganic support (aluminum oxide), and encapsulation in spherical calcium alginate beads via polyethylene glycol. Model dyes of 50 to 175 mg l(-1) were removed by the biocatalysts. Among the tested biocatalysts, the three with the highest specific activity and biodegradation rate were further studied (Chitosan-HRP, Al-GelHRP and Al-HRP-Gel). The impact of hydrogen peroxide concentration on dye decolorization was examined on the Chitosan-HRP biocatalyst, since the HRP is susceptible to inhibition/inactivation by high H2O2. On the other hand, H2O2 is needed as a co-substrate for the HRP, and the H2O2/dye ratio can greatly influence decolorization efficiency. Concentrations of H2O2 ranging from 0.22 to 4.4 mM showed no difference in terms of impact on the biocatalyst decolorization efficiency. The high decolorization efficiency of the biocatalysts was validated by the removal of 25 and 100 mg l(-1) anthraquinone (Remazol Brilliant Blue R (RBBR)), triphenylmethane (Coomassie Brilliant Blue CBB)), acridine (Acridine Orange (AO)), and formazan metal complex dye (Reactive Blue 52 (RB52)). After the seven consecutive decolorization cycles, the decolorization was still 53, 78, and 67% of the initial dye for the Al-HRP-Gel, Al-Gel-HRP, and Chitosan-HRP immobilizate, respectively. The results obtained showed potential of otherwise neglected acidic HRP isoforms as a cost-effective biocatalyst with significant potential in wastewater dyestuff treatment.
PB  - Springer Heidelberg, Heidelberg
T2  - Environmental Science and Pollution Research
T1  - Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes
VL  - 24
IS  - 4
SP  - 3923
EP  - 3933
DO  - 10.1007/s11356-016-8100-4
ER  - 

@article{
author = "Janović, Barbara and Vicovac, Milica Lj. Micic and Vujčić, Zoran and Vujčić, Miroslava",
year = "2017",
abstract = "Peroxidases (EC 1.11.1.7) have enormous biotechnological applications. Usage of more abundant, basic isoforms of peroxidases in diagnostic kits and/or in immunochemistry has led to under exploitation and disregard of horseradish peroxidase (HRP) acidic isoforms. Therefore, acidic horseradish peroxidase (HRP-A) isoenzymewas used for the preparation of a biocatalyst with improved ability in dye decolorization. Ten biocatalysts were prepared by covalent binding of enzyme to chitosan and alginate, adsorption followed by cross-linking on inorganic support (aluminum oxide), and encapsulation in spherical calcium alginate beads via polyethylene glycol. Model dyes of 50 to 175 mg l(-1) were removed by the biocatalysts. Among the tested biocatalysts, the three with the highest specific activity and biodegradation rate were further studied (Chitosan-HRP, Al-GelHRP and Al-HRP-Gel). The impact of hydrogen peroxide concentration on dye decolorization was examined on the Chitosan-HRP biocatalyst, since the HRP is susceptible to inhibition/inactivation by high H2O2. On the other hand, H2O2 is needed as a co-substrate for the HRP, and the H2O2/dye ratio can greatly influence decolorization efficiency. Concentrations of H2O2 ranging from 0.22 to 4.4 mM showed no difference in terms of impact on the biocatalyst decolorization efficiency. The high decolorization efficiency of the biocatalysts was validated by the removal of 25 and 100 mg l(-1) anthraquinone (Remazol Brilliant Blue R (RBBR)), triphenylmethane (Coomassie Brilliant Blue CBB)), acridine (Acridine Orange (AO)), and formazan metal complex dye (Reactive Blue 52 (RB52)). After the seven consecutive decolorization cycles, the decolorization was still 53, 78, and 67% of the initial dye for the Al-HRP-Gel, Al-Gel-HRP, and Chitosan-HRP immobilizate, respectively. The results obtained showed potential of otherwise neglected acidic HRP isoforms as a cost-effective biocatalyst with significant potential in wastewater dyestuff treatment.",
publisher = "Springer Heidelberg, Heidelberg",
journal = "Environmental Science and Pollution Research",
title = "Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes",
volume = "24",
number = "4",
pages = "3923-3933",
doi = "10.1007/s11356-016-8100-4"
}

Janović, B., Vicovac, M. Lj. M., Vujčić, Z.,& Vujčić, M.. (2017). Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes. in Environmental Science and Pollution Research
Springer Heidelberg, Heidelberg., 24(4), 3923-3933.
https://doi.org/10.1007/s11356-016-8100-4

Janović B, Vicovac MLM, Vujčić Z, Vujčić M. Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes. in Environmental Science and Pollution Research. 2017;24(4):3923-3933.
doi:10.1007/s11356-016-8100-4 .

Janović, Barbara, Vicovac, Milica Lj. Micic, Vujčić, Zoran, Vujčić, Miroslava, "Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes" in Environmental Science and Pollution Research, 24, no. 4 (2017):3923-3933,
https://doi.org/10.1007/s11356-016-8100-4 . .

TY  - JOUR
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1908
AB  - Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications.
PB  - Elsevier
T2  - Journal of Molecular Catalysis B: Enzymatic
T1  - Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
VL  - 134
SP  - 390
EP  - 395
DO  - 10.1016/j.molcatb.2016.06.005
ER  - 

@article{
author = "Lončar, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2016",
abstract = "Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications.",
publisher = "Elsevier",
journal = "Journal of Molecular Catalysis B: Enzymatic",
title = "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a",
volume = "134",
pages = "390-395",
doi = "10.1016/j.molcatb.2016.06.005"
}

Lončar, N., Božić, N.,& Vujčić, Z.. (2016). Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis B: Enzymatic
Elsevier., 134, 390-395.
https://doi.org/10.1016/j.molcatb.2016.06.005

Lončar N, Božić N, Vujčić Z. Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005 .

Lončar, Nikola, Božić, Nataša, Vujčić, Zoran, "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a" in Journal of Molecular Catalysis B: Enzymatic, 134 (2016):390-395,
https://doi.org/10.1016/j.molcatb.2016.06.005 . .