Vujčić, Zoran

Link to this page

Authority KeyName Variants
orcid::0000-0002-8963-2439
  • Vujčić, Zoran (110)
Projects
Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection Interakcije prirodnih proizvoda i njihovih analoga sa proteinima i nukleinskim kiselinama
Spanish MICINN [CTQ2011-28398-CO2-01] FEBS Collaborative Experimental Scholarship, Oslo, Norway
Mechanistic studies of the reactions of transition metal ion complexes with biologically relevant molecules project ApliMetaFarma [RC.2.2.08-0046]
STSM Grant from COST Action [BM1403] ICGEB [CRP/YUG11-02]
ICGEB research project [CRP/YUG11-02] The synthesis of aminoquinoline-based antimalarials and botulinum neurotoxin A inhibitors
Development of molecules with antiinflammatory and cardioprotective activity: structural modifications, modelling, physicochemical characterization and formulation investigations Biotechnology in vitro - crop, medicinal and endangered plant species
Microbial diversity study and characterization of beneficial environmental microorganisms Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry) Nanostructured Functional and Composite Materials in Catalytic and Sorption Processes
The Impact of Mining Wastes from RTB Bor on the Pollution of Surrounding Water Systems with the Proposal of Measures and Procedures for Reduction the Harmful Effects on the Environment International Centre for Genetic Engineering and Biotechnology (ICGEB) [CRP/YUG11-02]
Joint Serbian-Spanish Action Joint Serbian-Spanish Action [A IB2010 SE-00122]
Spanish MICINN [CTQ2008-00578] Austrian Science Fund (FWF) Project Number P 25613 B20 to ISD
Deutscher Akademischer Austausch Dienst (DAAD) Federation of European Biochemical Societies
ICGEB research [CRP/YUG11-02] ICGEB Research Grant [CRP/YUG11-02]
Study of structure-function relationships in the plant cell wall and modifications of the wall structure by enzyme engineering Interactive role of dyslipidemia, oxidative stress and inflammation in atherosclerosis and other diseases: genetic and biochemical markers
Antioxidative defense, differentiation and regeneration potential of tissue specific mesenchymal stem cells during ageing Regenerative and modulatory potential of adult stem cells

Author's Bibliography

Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines

Simić, Stefan; Jeremić, Sanja; Đokić, Lidija; Božić, Nataša; Vujčić, Zoran; Lončar, Nikola L.; Senthamaraikannan, Ramsankar; Babu, Ramesh P.; Opsenica, Igor; Nikodinović-Runić, Jasmina

(2020)

TY  - JOUR
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Lončar, Nikola L.
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh P.
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3356
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.
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
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 L. and Senthamaraikannan, Ramsankar and Babu, Ramesh P. and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3356",
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.",
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",
doi = "10.1016/j.enzmictec.2019.109411"
}
Simić, S., Jeremić, S., Đokić, L., Božić, N., Vujčić, Z., Lončar, N. L., 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.
Enzyme and Microbial Technology, 132.
https://doi.org/10.1016/j.enzmictec.2019.109411
Simić S, Jeremić S, Đokić L, Božić N, Vujčić Z, Lončar NL, 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. Enzyme and Microbial Technology. 2020;132
Simić Stefan, Jeremić Sanja, Đokić Lidija, Božić Nataša, Vujčić Zoran, Lončar Nikola L., Senthamaraikannan Ramsankar, Babu Ramesh P., Opsenica Igor, Nikodinović-Runić Jasmina, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" Enzyme and Microbial Technology, 132 (2020),
https://doi.org/10.1016/j.enzmictec.2019.109411 .
2
2
2

Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411

Simić, Stefan; Jeremić, Sanja; Đokić, Lidija; Božić, Nataša; Vujčić, Zoran; Lončar, Nikola L.; Senthamaraikannan, Ramsankar; Babu, Ramesh P.; Opsenica, Igor; Nikodinović-Runić, Jasmina

(2020)

TY  - BOOK
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Lončar, Nikola L.
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh P.
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3357
T2  - Enzyme and Microbial Technology
T1  - Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411
ER  - 
@book{
author = "Simić, Stefan and Jeremić, Sanja and Đokić, Lidija and Božić, Nataša and Vujčić, Zoran and Lončar, Nikola L. and Senthamaraikannan, Ramsankar and Babu, Ramesh P. and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3357",
journal = "Enzyme and Microbial Technology",
title = "Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411"
}
Simić, S., Jeremić, S., Đokić, L., Božić, N., Vujčić, Z., Lončar, N. L., Senthamaraikannan, R., Babu, R. P., Opsenica, I.,& Nikodinović-Runić, J. (2020). Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411.
Enzyme and Microbial Technology.
Simić S, Jeremić S, Đokić L, Božić N, Vujčić Z, Lončar NL, Senthamaraikannan R, Babu RP, Opsenica I, Nikodinović-Runić J. Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411. Enzyme and Microbial Technology. 2020;
Simić Stefan, Jeremić Sanja, Đokić Lidija, Božić Nataša, Vujčić Zoran, Lončar Nikola L., Senthamaraikannan Ramsankar, Babu Ramesh P., Opsenica Igor, Nikodinović-Runić Jasmina, "Supplementary data for article: Simić, S.; Jeremic, S.; Djokic, L.; Božić, N.; Vujčić, Z.; Lončar, N.; Senthamaraikannan, R.; Babu, R.; Opsenica, I. M.; Nikodinovic-Runic, J. Development of an Efficient Biocatalytic System Based on Bacterial Laccase for the Oxidation of Selected 1,4-Dihydropyridines. Enzyme and Microbial Technology 2020, 132. https://doi.org/10.1016/j.enzmictec.2019.109411" Enzyme and Microbial Technology (2020)

Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase

Božić, Nataša; Rozeboom, Henriëtte J.; Lončar, Nikola; Šokarda Slavić, Marinela; Janssen, Dick B.; Vujčić, Zoran

(Elsevier, 2020)

TY  - JOUR
AU  - Božić, Nataša
AU  - Rozeboom, Henriëtte J.
AU  - Lončar, Nikola
AU  - Šokarda Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4261
AB  - α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase
VL  - 165
IS  - A
SP  - 1529
EP  - 1539
DO  - 10.1016/j.ijbiomac.2020.10.025
ER  - 
@article{
author = "Božić, Nataša and Rozeboom, Henriëtte J. and Lončar, Nikola and Šokarda Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4261",
abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase",
volume = "165",
number = "A",
pages = "1529-1539",
doi = "10.1016/j.ijbiomac.2020.10.025"
}
Božić, N., Rozeboom, H. J., Lončar, N., Šokarda Slavić, M., Janssen, D. B.,& Vujčić, Z. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase.
International Journal of Biological Macromolecules
Elsevier., 165(A), 1529-1539.
https://doi.org/10.1016/j.ijbiomac.2020.10.025
Božić N, Rozeboom HJ, Lončar N, Šokarda Slavić M, Janssen DB, Vujčić Z. Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. International Journal of Biological Macromolecules. 2020;165(A):1529-1539
Božić Nataša, Rozeboom Henriëtte J., Lončar Nikola, Šokarda Slavić Marinela, Janssen Dick B., Vujčić Zoran, "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase" International Journal of Biological Macromolecules, 165, no. A (2020):1529-1539,
https://doi.org/10.1016/j.ijbiomac.2020.10.025 .
2

Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase

Božić, Nataša; Rozeboom, Henriëtte J.; Lončar, Nikola; Šokarda Slavić, Marinela; Janssen, Dick B.; Vujčić, Zoran

(Elsevier, 2020)

TY  - JOUR
AU  - Božić, Nataša
AU  - Rozeboom, Henriëtte J.
AU  - Lončar, Nikola
AU  - Šokarda Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4262
AB  - α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase
VL  - 165
IS  - A
SP  - 1529
EP  - 1539
DO  - 10.1016/j.ijbiomac.2020.10.025
ER  - 
@article{
author = "Božić, Nataša and Rozeboom, Henriëtte J. and Lončar, Nikola and Šokarda Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4262",
abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase",
volume = "165",
number = "A",
pages = "1529-1539",
doi = "10.1016/j.ijbiomac.2020.10.025"
}
Božić, N., Rozeboom, H. J., Lončar, N., Šokarda Slavić, M., Janssen, D. B.,& Vujčić, Z. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase.
International Journal of Biological Macromolecules
Elsevier., 165(A), 1529-1539.
https://doi.org/10.1016/j.ijbiomac.2020.10.025
Božić N, Rozeboom HJ, Lončar N, Šokarda Slavić M, Janssen DB, Vujčić Z. Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. International Journal of Biological Macromolecules. 2020;165(A):1529-1539
Božić Nataša, Rozeboom Henriëtte J., Lončar Nikola, Šokarda Slavić Marinela, Janssen Dick B., Vujčić Zoran, "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase" International Journal of Biological Macromolecules, 165, no. A (2020):1529-1539,
https://doi.org/10.1016/j.ijbiomac.2020.10.025 .
2

Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1

Lončar, Nikola L.; Drašković, Natalija; Božić, Nataša; Romero, Elvira; Simić, Stefan; Opsenica, Igor; Vujčić, Zoran; Fraaije, Marco W.

(MDPI, 2019)

TY  - JOUR
AU  - Lončar, Nikola L.
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  - http://cherry.chem.bg.ac.rs/handle/123456789/3709
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 efficiency of dyeing processes is still poor and results in large amounts of colored effluents. 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 (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP 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 Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP 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
IS  - 5
DO  - 10.3390/catal9050463
ER  - 
@article{
author = "Lončar, Nikola L. and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3709",
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 efficiency of dyeing processes is still poor and results in large amounts of colored effluents. 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 (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP 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 Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP 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",
number = "5",
doi = "10.3390/catal9050463"
}
Lončar, N. L., 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.
Catalysts
MDPI., 9(5).
https://doi.org/10.3390/catal9050463
Lončar NL, 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. Catalysts. 2019;9(5)
Lončar Nikola L., 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" Catalysts, 9, no. 5 (2019),
https://doi.org/10.3390/catal9050463 .
1
4
2
4

Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463

Lončar, Nikola L.; Drašković, Natalija; Božić, Nataša; Romero, Elvira; Simić, Stefan; Opsenica, Igor; Vujčić, Zoran; Fraaije, Marco W.

(MDPI, 2019)

TY  - BOOK
AU  - Lončar, Nikola L.
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  - http://cherry.chem.bg.ac.rs/handle/123456789/3710
PB  - MDPI
T2  - Catalysts
T1  - Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463
ER  - 
@book{
author = "Lončar, Nikola L. and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3710",
publisher = "MDPI",
journal = "Catalysts",
title = "Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463"
}
Lončar, N. L., Drašković, N., Božić, N., Romero, E., Simić, S., Opsenica, I., Vujčić, Z.,& Fraaije, M. W. (2019). Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463.
Catalysts
MDPI..
Lončar NL, Drašković N, Božić N, Romero E, Simić S, Opsenica I, Vujčić Z, Fraaije MW. Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463. Catalysts. 2019;
Lončar Nikola L., Drašković Natalija, Božić Nataša, Romero Elvira, Simić Stefan, Opsenica Igor, Vujčić Zoran, Fraaije Marco W., "Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463" Catalysts (2019)

Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw

Grujić, Marica; Dojnov, Biljana; Potočnik, Ivana; Atanasova, Lea; Duduk, Bojan; Srebotnik, Ewald; Druzhinina, Irirna S.; Kubicek, Christian P.; Vujčić, Zoran

(Springer Link, 2019)

TY  - JOUR
AU  - Grujić, Marica
AU  - Dojnov, Biljana
AU  - Potočnik, Ivana
AU  - Atanasova, Lea
AU  - Duduk, Bojan
AU  - Srebotnik, Ewald
AU  - Druzhinina, Irirna S.
AU  - Kubicek, Christian P.
AU  - Vujčić, Zoran
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3768
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 Link
T2  - World Journal of Microbiology and Biotechnology
T1  - Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw
VL  - 35
IS  - 12
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, Irirna S. and Kubicek, Christian P. and Vujčić, Zoran",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3768",
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 Link",
journal = "World Journal of Microbiology and Biotechnology",
title = "Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw",
volume = "35",
number = "12",
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.
World Journal of Microbiology and Biotechnology
Springer Link., 35(12).
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. World Journal of Microbiology and Biotechnology. 2019;35(12)
Grujić Marica, Dojnov Biljana, Potočnik Ivana, Atanasova Lea, Duduk Bojan, Srebotnik Ewald, Druzhinina Irirna S., Kubicek Christian P., Vujčić Zoran, "Superior cellulolytic activity of Trichoderma guizhouense on raw wheat straw" World Journal of Microbiology and Biotechnology, 35, no. 12 (2019),
https://doi.org/10.1007/s11274-019-2774-y .
6
3
5

Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins

Nišavić, Marija; Janjić, Goran V.; Hozić, Amela; Petković, Marijana; Milčić, Miloš K.; Vujčić, Zoran; Cindrić, Mario

(Royal Soc Chemistry, Cambridge, 2018)

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3243
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/c7mt00330g
ER  - 
@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3243",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/c7mt00330g"
}
Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins.
Metallomics
Royal Soc Chemistry, Cambridge., 10(4), 587-594.
https://doi.org/10.1039/c7mt00330g
Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. Metallomics. 2018;10(4):587-594
Nišavić Marija, Janjić Goran V., Hozić Amela, Petković Marijana, Milčić Miloš K., Vujčić Zoran, Cindrić Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/c7mt00330g .
1
5
5
6

Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g

Nišavić, Marija; Janjić, Goran V.; Hozić, Amela; Petković, Marijana; Milčić, Miloš K.; Vujčić, Zoran; Cindrić, Mario

(Royal Soc Chemistry, Cambridge, 2018)

TY  - BOOK
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3244
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g
ER  - 
@book{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3244",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g"
}
Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M. (2018). Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g.
Metallomics
Royal Soc Chemistry, Cambridge..
Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g. Metallomics. 2018;
Nišavić Marija, Janjić Goran V., Hozić Amela, Petković Marijana, Milčić Miloš K., Vujčić Zoran, Cindrić Mario, "Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g" Metallomics (2018)

Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2

Tadić, Vojin; Tadić, Jovan; Milošević, Snežana; Cingel, Aleksandar; Prodanović, Olivera; Ćosić, Tatjana; Vujčić, Zoran

(Elsevier Science Bv, Amsterdam, 2018)

TY  - JOUR
AU  - Tadić, Vojin
AU  - Tadić, Jovan
AU  - Milošević, Snežana
AU  - Cingel, Aleksandar
AU  - Prodanović, Olivera
AU  - Ćosić, Tatjana
AU  - Vujčić, Zoran
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2090
AB  - In this study we investigated physiological parameters of stress (enzymatic and non-enzymatic) in lettuce (Lactuca sativa L.) and its hairy roots induced by water solution of phenol. Two varieties of lettuce were examined, Ljubljanska ledenka and Nansen. Plants were grown in water with phenol concentration of 200 mgL(-1), during 10 days. We monitored activity of peroxidases, catalases, polyphenol oxidase and superoxide dismutase, as well as proline and chlorophyll content. We observed a decrease in peroxidases, and increase in activity of catalase, polyphenol oxidase and superoxide dismutase compared to control plants. The concentration of praline was constantly increasing in both lettuce varieties over the course of the experiment. We detected an increase in activity of all monitored enzymes, except polyphenol oxidases, in hairy roots. The hydroponic system provides a useful framework for studying the effect of different harmful substances and its elimination. In such a system, as used in this work for the study of physiological processes in antioxidant protection activated when plant was exposed to phenol, lettuce and its hairy roots can be viewed as tools for water remediation.
PB  - Elsevier Science Bv, Amsterdam
T2  - Scientia Horticulturae
T1  - Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2
VL  - 232
SP  - 71
EP  - 83
DO  - 10.1016/j.scienta.2017.12.024
ER  - 
@article{
author = "Tadić, Vojin and Tadić, Jovan and Milošević, Snežana and Cingel, Aleksandar and Prodanović, Olivera and Ćosić, Tatjana and Vujčić, Zoran",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2090",
abstract = "In this study we investigated physiological parameters of stress (enzymatic and non-enzymatic) in lettuce (Lactuca sativa L.) and its hairy roots induced by water solution of phenol. Two varieties of lettuce were examined, Ljubljanska ledenka and Nansen. Plants were grown in water with phenol concentration of 200 mgL(-1), during 10 days. We monitored activity of peroxidases, catalases, polyphenol oxidase and superoxide dismutase, as well as proline and chlorophyll content. We observed a decrease in peroxidases, and increase in activity of catalase, polyphenol oxidase and superoxide dismutase compared to control plants. The concentration of praline was constantly increasing in both lettuce varieties over the course of the experiment. We detected an increase in activity of all monitored enzymes, except polyphenol oxidases, in hairy roots. The hydroponic system provides a useful framework for studying the effect of different harmful substances and its elimination. In such a system, as used in this work for the study of physiological processes in antioxidant protection activated when plant was exposed to phenol, lettuce and its hairy roots can be viewed as tools for water remediation.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Scientia Horticulturae",
title = "Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2",
volume = "232",
pages = "71-83",
doi = "10.1016/j.scienta.2017.12.024"
}
Tadić, V., Tadić, J., Milošević, S., Cingel, A., Prodanović, O., Ćosić, T.,& Vujčić, Z. (2018). Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2.
Scientia Horticulturae
Elsevier Science Bv, Amsterdam., 232, 71-83.
https://doi.org/10.1016/j.scienta.2017.12.024
Tadić V, Tadić J, Milošević S, Cingel A, Prodanović O, Ćosić T, Vujčić Z. Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2. Scientia Horticulturae. 2018;232:71-83
Tadić Vojin, Tadić Jovan, Milošević Snežana, Cingel Aleksandar, Prodanović Olivera, Ćosić Tatjana, Vujčić Zoran, "Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2" Scientia Horticulturae, 232 (2018):71-83,
https://doi.org/10.1016/j.scienta.2017.12.024 .

Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties

Miočinović, Jelena; Tomić, Nikola; Dojnov, Biljana; Tomašević, Igor; Stojanović, Sanja; Đekić, Ilija; Vujčić, Zoran

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Miočinović, Jelena
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Tomašević, Igor
AU  - Stojanović, Sanja
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2080
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. (c) 2017 Society of Chemical Industry
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 = "Miočinović, Jelena and Tomić, Nikola and Dojnov, Biljana and Tomašević, Igor and Stojanović, Sanja and Đekić, Ilija and Vujčić, Zoran",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2080",
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. (c) 2017 Society of Chemical Industry",
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"
}
Miočinović, J., Tomić, N., Dojnov, B., Tomašević, 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.
Journal of the Science of Food and Agriculture
Wiley, Hoboken., 98(4), 1291-1299.
https://doi.org/10.1002/jsfa.8592
Miočinović J, Tomić N, Dojnov B, Tomašević 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. Journal of the Science of Food and Agriculture. 2018;98(4):1291-1299
Miočinović Jelena, Tomić Nikola, Dojnov Biljana, Tomašević 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" Journal of the Science of Food and Agriculture, 98, no. 4 (2018):1291-1299,
https://doi.org/10.1002/jsfa.8592 .
10
9
9

Application of new insoluble dietary fibres from triticale as supplement in yoghurt - effects on physico-chemical, rheological and quality properties

Miočinović, Jelena; Tomić, Nikola; Dojnov, Biljana; Tomašević, Igor; Stojanović, Sanja; Đekić, Ilija; Vujčić, Zoran

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Miočinović, Jelena
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Tomašević, Igor
AU  - Stojanović, Sanja
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3171
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. (c) 2017 Society of Chemical Industry
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 = "Miočinović, Jelena and Tomić, Nikola and Dojnov, Biljana and Tomašević, Igor and Stojanović, Sanja and Đekić, Ilija and Vujčić, Zoran",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3171",
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. (c) 2017 Society of Chemical Industry",
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"
}
Miočinović, J., Tomić, N., Dojnov, B., Tomašević, 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.
Journal of the Science of Food and Agriculture
Wiley, Hoboken., 98(4), 1291-1299.
https://doi.org/10.1002/jsfa.8592
Miočinović J, Tomić N, Dojnov B, Tomašević 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. Journal of the Science of Food and Agriculture. 2018;98(4):1291-1299
Miočinović Jelena, Tomić Nikola, Dojnov Biljana, Tomašević 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" Journal of the Science of Food and Agriculture, 98, no. 4 (2018):1291-1299,
https://doi.org/10.1002/jsfa.8592 .
10
9
10

Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins

Nišavić, Marija; Janjić, Goran V.; Hozić, Amela; Petković, Marijana; Milčić, Miloš K.; Vujčić, Zoran; Cindrić, Mario

(Royal Soc Chemistry, Cambridge, 2018)

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2134
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/c7mt00330g
ER  - 
@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2134",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/c7mt00330g"
}
Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins.
Metallomics
Royal Soc Chemistry, Cambridge., 10(4), 587-594.
https://doi.org/10.1039/c7mt00330g
Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. Metallomics. 2018;10(4):587-594
Nišavić Marija, Janjić Goran V., Hozić Amela, Petković Marijana, Milčić Miloš K., Vujčić Zoran, Cindrić Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/c7mt00330g .
1
5
5
6

Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1

Tadić, Vojin; Petric, Marija; Uzelac, Branka; Milošević, Snežana; Vujčić, Zoran; Stevanovic, Jasmina; Tadić, Jovan

(Elsevier Science Bv, Amsterdam, 2018)

TY  - JOUR
AU  - Tadić, Vojin
AU  - Petric, Marija
AU  - Uzelac, Branka
AU  - Milošević, Snežana
AU  - Vujčić, Zoran
AU  - Stevanovic, Jasmina
AU  - Tadić, Jovan
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2106
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 Science Bv, Amsterdam
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 Petric, Marija and Uzelac, Branka and Milošević, Snežana and Vujčić, Zoran and Stevanovic, Jasmina and Tadić, Jovan",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2106",
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 Science Bv, Amsterdam",
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., Petric, M., Uzelac, B., Milošević, S., Vujčić, Z., Stevanovic, J.,& Tadić, J. (2018). Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1.
Scientia Horticulturae
Elsevier Science Bv, Amsterdam., 231, 210-218.
https://doi.org/10.1016/j.scienta.2017.12.025
Tadić V, Petric M, Uzelac B, Milošević S, Vujčić Z, Stevanovic J, Tadić J. Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1. Scientia Horticulturae. 2018;231:210-218
Tadić Vojin, Petric Marija, Uzelac Branka, Milošević Snežana, Vujčić Zoran, Stevanovic Jasmina, Tadić Jovan, "Phenol removal from solution using different varieties of lettuce (Lactuca sativa L.) - Part 1" Scientia Horticulturae, 231 (2018):210-218,
https://doi.org/10.1016/j.scienta.2017.12.025 .
3
2
2

Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective

Tomić, Nikola; Dojnov, Biljana; Miočinović, Jelena; Tomašević, Igor; Smigić, Nada; Đekić, Ilija; Vujčić, Zoran

(Elsevier Science Bv, Amsterdam, 2017)

TY  - JOUR
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Miočinović, Jelena
AU  - Tomašević, Igor
AU  - Smigić, Nada
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2451
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 Science Bv, Amsterdam
T2  - LWT -food Science and Technology ( Lebensmittel - Wissenschaft und Technologie)
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 Miočinović, Jelena and Tomašević, Igor and Smigić, Nada and Đekić, Ilija and Vujčić, Zoran",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2451",
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 Science Bv, Amsterdam",
journal = "LWT -food Science and Technology ( Lebensmittel - Wissenschaft und Technologie)",
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., Miočinović, J., Tomašević, I., Smigić, N., Đekić, I.,& Vujčić, Z. (2017). Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective.
LWT -food Science and Technology ( Lebensmittel - Wissenschaft und Technologie)
Elsevier Science Bv, Amsterdam., 80, 59-66.
https://doi.org/10.1016/j.lwt.2017.02.008
Tomić N, Dojnov B, Miočinović J, Tomašević I, Smigić N, Đekić I, Vujčić Z. Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective. LWT -food Science and Technology ( Lebensmittel - Wissenschaft und Technologie). 2017;80:59-66
Tomić Nikola, Dojnov Biljana, Miočinović Jelena, Tomašević Igor, Smigić Nada, Đekić Ilija, Vujčić Zoran, "Enrichment of yoghurt with insoluble dietary fiber from triticale - A sensory perspective" LWT -food Science and Technology ( Lebensmittel - Wissenschaft und Technologie), 80 (2017):59-66,
https://doi.org/10.1016/j.lwt.2017.02.008 .
23
14
18

Enrichment of yoghurt with insoluble dietary fiber from triticale – A sensory perspective

Tomić, Nikola; Dojnov, Biljana; Miočinović, Jelena; Tomašević, Igor; Smigić, Nada; Đekić, Ilija; Vujčić, Zoran

(Elsevier Science Bv, Amsterdam, 2017)

TY  - JOUR
AU  - Tomić, Nikola
AU  - Dojnov, Biljana
AU  - Miočinović, Jelena
AU  - Tomašević, Igor
AU  - Smigić, Nada
AU  - Đekić, Ilija
AU  - Vujčić, Zoran
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3091
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 Science Bv, Amsterdam
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 Miočinović, Jelena and Tomašević, Igor and Smigić, Nada and Đekić, Ilija and Vujčić, Zoran",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3091",
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 Science Bv, Amsterdam",
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., Miočinović, J., Tomašević, I., Smigić, N., Đekić, I.,& Vujčić, Z. (2017). Enrichment of yoghurt with insoluble dietary fiber from triticale – A sensory perspective.
LWT - Food Science and Technology
Elsevier Science Bv, Amsterdam., 80, 59-66.
https://doi.org/10.1016/j.lwt.2017.02.008
Tomić N, Dojnov B, Miočinović J, Tomašević I, Smigić N, Đekić I, Vujčić Z. Enrichment of yoghurt with insoluble dietary fiber from triticale – A sensory perspective. LWT - Food Science and Technology. 2017;80:59-66
Tomić Nikola, Dojnov Biljana, Miočinović Jelena, Tomašević Igor, Smigić Nada, Đekić Ilija, Vujčić Zoran, "Enrichment of yoghurt with insoluble dietary fiber from triticale – A sensory perspective" LWT - Food Science and Technology, 80 (2017):59-66,
https://doi.org/10.1016/j.lwt.2017.02.008 .
23
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19

Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes

Janović, Barbara; Collins, Andrew R.; Vujčić, Zoran; Vujčić, Miroslava

(Elsevier Science Bv, Amsterdam, 2017)

TY  - JOUR
AU  - Janović, Barbara
AU  - Collins, Andrew R.
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3189
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. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3189",
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. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
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.
Journal of Hazardous Materials
Elsevier Science Bv, Amsterdam., 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. Journal of Hazardous Materials. 2017;321:576-585
Janović Barbara, Collins Andrew R., Vujčić Zoran, Vujčić Miroslava, "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes" Journal of Hazardous Materials, 321 (2017):576-585,
https://doi.org/10.1016/j.jhazmat.2016.09.037 .
4
3
4

Supplementary material for the article: Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037

Janović, Barbara; Collins, Andrew R.; Vujčić, Zoran; Vujčić, Miroslava

(Elsevier Science Bv, Amsterdam, 2017)

TY  - BOOK
AU  - Janović, Barbara
AU  - Collins, Andrew R.
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3190
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Hazardous Materials
T1  - Supplementary material for the article:           Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037
ER  - 
@book{
author = "Janović, Barbara and Collins, Andrew R. and Vujčić, Zoran and Vujčić, Miroslava",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3190",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Hazardous Materials",
title = "Supplementary material for the article:           Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037"
}
Janović, B., Collins, A. R., Vujčić, Z.,& Vujčić, M. (2017). Supplementary material for the article:           Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037.
Journal of Hazardous Materials
Elsevier Science Bv, Amsterdam..
Janović B, Collins AR, Vujčić Z, Vujčić M. Supplementary material for the article:           Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037. Journal of Hazardous Materials. 2017;
Janović Barbara, Collins Andrew R., Vujčić Zoran, Vujčić Miroslava, "Supplementary material for the article:           Janović, B. S.; Collins, A. R.; Vujčić, Z. M.; Vujčić, M. T. Acidic Horseradish Peroxidase Activity Abolishes Genotoxicity of Common Dyes. Journal of Hazardous Materials 2017, 321, 576–585. https://doi.org/10.1016/j.jhazmat.2016.09.037" Journal of Hazardous Materials (2017)

Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes

Janović, Barbara; Collins, Andrew R.; Vujčić, Zoran; Vujčić, Miroslava

(Elsevier Science Bv, Amsterdam, 2017)

TY  - JOUR
AU  - Janović, Barbara
AU  - Collins, Andrew R.
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2356
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. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2356",
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. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
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.
Journal of Hazardous Materials
Elsevier Science Bv, Amsterdam., 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. Journal of Hazardous Materials. 2017;321:576-585
Janović Barbara, Collins Andrew R., Vujčić Zoran, Vujčić Miroslava, "Acidic horseradish peroxidase activity abolishes genotoxicity of common dyes" Journal of Hazardous Materials, 321 (2017):576-585,
https://doi.org/10.1016/j.jhazmat.2016.09.037 .
4
3
4

Tailor-made biocatalysts based on scarcely studied acidic horseradish peroxidase for biodegradation of reactive dyes

Janović, Barbara; Vicovac, Milica Lj. Micic; Vujčić, Zoran; Vujčić, Miroslava

(Springer Heidelberg, Heidelberg, 2017)

TY  - JOUR
AU  - Janović, Barbara
AU  - Vicovac, Milica Lj. Micic
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2435
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2435",
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.
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. Environmental Science and Pollution Research. 2017;24(4):3923-3933
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" Environmental Science and Pollution Research, 24, no. 4 (2017):3923-3933,
https://doi.org/10.1007/s11356-016-8100-4 .
7
7
8

Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae

Margetić, Aleksandra; Vujčić, Zoran

(Taylor & Francis Inc, Philadelphia, 2017)

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2433
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 and 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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2433",
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 and 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.
Preparative Biochemistry and 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. Preparative Biochemistry and Biotechnology. 2017;47(3):305-311
Margetić Aleksandra, Vujčić Zoran, "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae" Preparative Biochemistry and Biotechnology, 47, no. 3 (2017):305-311,
https://doi.org/10.1080/10826068.2016.1244683 .
7
5
7

Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base

Petric, Marija; Subotic, Angelina; Jevremovic, Sladana; Trifunović-Momcilov, Milana; Tadić, Vojin; Grujić, Marica; Vujčić, Zoran

(Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd, 2017)

TY  - JOUR
AU  - Petric, Marija
AU  - Subotic, Angelina
AU  - Jevremovic, Sladana
AU  - Trifunović-Momcilov, Milana
AU  - Tadić, Vojin
AU  - Grujić, Marica
AU  - Vujčić, Zoran
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2543
AB  - The aim of this study was to determine the enzymatic profile of esterases and peroxidases during early stages of somatic embryogenesis of Fritillaria meleagris L. Somatic embryogenesis was induced using the leaf base as explant on a medium supplemented with 2,4-dichlorophenoxyacetic acid (2,4-D). Zymography showed the presence of different moieties, six isoforms of esterases and peroxidases, during morphogenesis as compared to control explants. One isoform of esterases was detected only during the process of somatic embryogenesis, and one isoform was detected in control explants. Analysis of esterases with 1-naphthyl butyrate proved that esterases, which participate in somatic embryogenesis of F. meleagris, belong to the family of aryl esterases. For the first time it was proved that five isoforms of esterases, which are involved in morphogenesis of F. meleagris, belong to the family of aryl esterases, while two isoforms are carboxyl esterases. One isoform of carboxyl esterases was visible in control explants. This is also the first description of peroxidases during the morphogenetic process, and of the difference between aryl and carboxyl esterases. More isoforms of esterases during morphogenesis as compared to control explants are probably responsible for some early physiological process during somatic embryogenesis of F. meleagris.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base
VL  - 69
IS  - 4
SP  - 619
EP  - 625
DO  - 10.2298/ABS161130007P
ER  - 
@article{
author = "Petric, Marija and Subotic, Angelina and Jevremovic, Sladana and Trifunović-Momcilov, Milana and Tadić, Vojin and Grujić, Marica and Vujčić, Zoran",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2543",
abstract = "The aim of this study was to determine the enzymatic profile of esterases and peroxidases during early stages of somatic embryogenesis of Fritillaria meleagris L. Somatic embryogenesis was induced using the leaf base as explant on a medium supplemented with 2,4-dichlorophenoxyacetic acid (2,4-D). Zymography showed the presence of different moieties, six isoforms of esterases and peroxidases, during morphogenesis as compared to control explants. One isoform of esterases was detected only during the process of somatic embryogenesis, and one isoform was detected in control explants. Analysis of esterases with 1-naphthyl butyrate proved that esterases, which participate in somatic embryogenesis of F. meleagris, belong to the family of aryl esterases. For the first time it was proved that five isoforms of esterases, which are involved in morphogenesis of F. meleagris, belong to the family of aryl esterases, while two isoforms are carboxyl esterases. One isoform of carboxyl esterases was visible in control explants. This is also the first description of peroxidases during the morphogenetic process, and of the difference between aryl and carboxyl esterases. More isoforms of esterases during morphogenesis as compared to control explants are probably responsible for some early physiological process during somatic embryogenesis of F. meleagris.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base",
volume = "69",
number = "4",
pages = "619-625",
doi = "10.2298/ABS161130007P"
}
Petric, M., Subotic, A., Jevremovic, S., Trifunović-Momcilov, M., Tadić, V., Grujić, M.,& Vujčić, Z. (2017). Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base.
Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 69(4), 619-625.
https://doi.org/10.2298/ABS161130007P
Petric M, Subotic A, Jevremovic S, Trifunović-Momcilov M, Tadić V, Grujić M, Vujčić Z. Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base. Archives of biological sciences. 2017;69(4):619-625
Petric Marija, Subotic Angelina, Jevremovic Sladana, Trifunović-Momcilov Milana, Tadić Vojin, Grujić Marica, Vujčić Zoran, "Esterase and peroxidase isoforms during initial stages of somatic embryogenesis in Fritillaria meleagris L. leaf base" Archives of biological sciences, 69, no. 4 (2017):619-625,
https://doi.org/10.2298/ABS161130007P .

Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4

Šokarda-Slavić, Marinela; Pešić, Milja; Vujčić, Zoran; Božić, Nataša

(Springer, New York, 2016)

TY  - BOOK
AU  - Šokarda-Slavić, Marinela
AU  - Pešić, Milja
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3588
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4
ER  - 
@book{
author = "Šokarda-Slavić, Marinela and Pešić, Milja and Vujčić, Zoran and Božić, Nataša",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3588",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4"
}
Šokarda-Slavić, M., Pešić, M., Vujčić, Z.,& Božić, N. (2016). Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4.
Applied Microbiology and Biotechnology
Springer, New York..
Šokarda-Slavić M, Pešić M, Vujčić Z, Božić N. Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4. Applied Microbiology and Biotechnology. 2016;
Šokarda-Slavić Marinela, Pešić Milja, Vujčić Zoran, Božić Nataša, "Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4" Applied Microbiology and Biotechnology (2016)

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Lončar, Nikola L.; Božić, Nataša; Vujčić, Zoran

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3517
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. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
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 L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3517",
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. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
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. L., Božić, N.,& Vujčić, Z. (2016). Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a.
Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam., 134, 390-395.
https://doi.org/10.1016/j.molcatb.2016.06.005
Lončar NL, Božić N, Vujčić Z. Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395
Lončar Nikola L., Božić Nataša, Vujčić Zoran, "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a" Journal of Molecular Catalysis. B: Enzymatic, 134 (2016):390-395,
https://doi.org/10.1016/j.molcatb.2016.06.005 .
13
11
12

Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005

Lončar, Nikola L.; Božić, Nataša; Vujčić, Zoran

(Elsevier Science Bv, Amsterdam, 2016)

TY  - BOOK
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3518
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005
ER  - 
@book{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3518",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005"
}
Lončar, N. L., Božić, N.,& Vujčić, Z. (2016). Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005.
Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam..
Lončar NL, Božić N, Vujčić Z. Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005. Journal of Molecular Catalysis. B: Enzymatic. 2016;
Lončar Nikola L., Božić Nataša, Vujčić Zoran, "Supplementary data for the article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005" Journal of Molecular Catalysis. B: Enzymatic (2016)