TY  - DATA
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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3357
ER  - 

@misc{
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",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3357"
}

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. in Enzyme and Microbial Technology.
https://hdl.handle.net/21.15107/rcub_cherry_3357

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. in Enzyme and Microbial Technology. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_3357 .

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" in Enzyme and Microbial Technology (2020),
https://hdl.handle.net/21.15107/rcub_cherry_3357 .

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  - https://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",
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. in 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. in Enzyme and Microbial Technology. 2020;132.
doi: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, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" in Enzyme and Microbial Technology, 132 (2020),
https://doi.org/10.1016/j.enzmictec.2019.109411 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Rozeboom, Henriëtte J.
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - https://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 L. and Šokarda-Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
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. L., Šokarda-Slavić, M., Janssen, D. B.,& Vujčić, Z.. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. in 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 NL, Šokarda-Slavić M, Janssen DB, Vujčić Z. Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. in International Journal of Biological Macromolecules. 2020;165(A):1529-1539.
doi:10.1016/j.ijbiomac.2020.10.025 .

Božić, Nataša, Rozeboom, Henriëtte J., Lončar, Nikola L., Šokarda-Slavić, Marinela, Janssen, Dick B., Vujčić, Zoran, "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase" in International Journal of Biological Macromolecules, 165, no. A (2020):1529-1539,
https://doi.org/10.1016/j.ijbiomac.2020.10.025 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Rozeboom, Henriëtte J.
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - https://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 L. and Šokarda-Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
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. L., Šokarda-Slavić, M., Janssen, D. B.,& Vujčić, Z.. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. in 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 NL, Šokarda-Slavić M, Janssen DB, Vujčić Z. Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. in International Journal of Biological Macromolecules. 2020;165(A):1529-1539.
doi:10.1016/j.ijbiomac.2020.10.025 .

Božić, Nataša, Rozeboom, Henriëtte J., Lončar, Nikola L., Šokarda-Slavić, Marinela, Janssen, Dick B., Vujčić, Zoran, "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase" in International Journal of Biological Macromolecules, 165, no. A (2020):1529-1539,
https://doi.org/10.1016/j.ijbiomac.2020.10.025 . .

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  - https://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",
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. in 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. in Catalysts. 2019;9(5).
doi:10.3390/catal9050463 .

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" in Catalysts, 9, no. 5 (2019),
https://doi.org/10.3390/catal9050463 . .

TY  - DATA
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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3710
ER  - 

@misc{
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",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3710"
}

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. in Catalysts
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_3710

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. in Catalysts. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3710 .

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" in Catalysts (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3710 .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2375
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",
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. in 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. in Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005 .

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

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://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",
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. in 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. in Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005 .

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

TY  - DATA
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3518
ER  - 

@misc{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3518"
}

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. in Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3518

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. in Journal of Molecular Catalysis. B: Enzymatic. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3518 .

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" in Journal of Molecular Catalysis. B: Enzymatic (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3518 .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Colpa, Dana I.
AU  - Fraaije, Marco W.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2342
AB  - Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Tetrahedron
T1  - Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
VL  - 72
IS  - 46
SP  - 7276
EP  - 7281
DO  - 10.1016/j.tet.2015.12.078
ER  - 

@article{
author = "Lončar, Nikola L. and Colpa, Dana I. and Fraaije, Marco W.",
year = "2016",
abstract = "Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Tetrahedron",
title = "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase",
volume = "72",
number = "46",
pages = "7276-7281",
doi = "10.1016/j.tet.2015.12.078"
}

Lončar, N. L., Colpa, D. I.,& Fraaije, M. W.. (2016). Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron
Pergamon-Elsevier Science Ltd, Oxford., 72(46), 7276-7281.
https://doi.org/10.1016/j.tet.2015.12.078

Lončar NL, Colpa DI, Fraaije MW. Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron. 2016;72(46):7276-7281.
doi:10.1016/j.tet.2015.12.078 .

Lončar, Nikola L., Colpa, Dana I., Fraaije, Marco W., "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase" in Tetrahedron, 72, no. 46 (2016):7276-7281,
https://doi.org/10.1016/j.tet.2015.12.078 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Janović, Barbara
AU  - Lončar, Nikola L.
AU  - Margetić, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1644
AB  - Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization
VL  - 97
SP  - 124
EP  - 127
DO  - 10.1016/j.ibiod.2014.10.007
ER  - 

@article{
author = "Vujčić, Zoran and Janović, Barbara and Lončar, Nikola L. and Margetić, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava",
year = "2015",
abstract = "Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization",
volume = "97",
pages = "124-127",
doi = "10.1016/j.ibiod.2014.10.007"
}

Vujčić, Z., Janović, B., Lončar, N. L., Margetić, A., Božić, N., Dojnov, B.,& Vujčić, M.. (2015). Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 97, 124-127.
https://doi.org/10.1016/j.ibiod.2014.10.007

Vujčić Z, Janović B, Lončar NL, Margetić A, Božić N, Dojnov B, Vujčić M. Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation. 2015;97:124-127.
doi:10.1016/j.ibiod.2014.10.007 .

Vujčić, Zoran, Janović, Barbara, Lončar, Nikola L., Margetić, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization" in International Biodeterioration and Biodegradation, 97 (2015):124-127,
https://doi.org/10.1016/j.ibiod.2014.10.007 . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1985
AB  - Bacillus licheniformis 9945a alpha-amylase is known as a potent enzyme for raw starch hydrolysis. In this paper, a mixed mode Nuvia cPrime (TM) resin is examined with the aim to improve the downstream processing of raw starch digesting amylases and exploit the hydrophobic patches on their surface. This resin combines hydrophobic interactions with cation exchange groups and as such the presence of salt facilitates hydrophobic interactions while the ion-exchange groups enable proper selectivity. alpha-Amylase was produced using an optimized fed-batch approach in a defined media and significant overexpression of 1.2 g L-1 was achieved. This single step procedure enables simultaneous concentration, pigment removal as well as purification of amylase with yields of 96% directly from the fermentation broth.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases
VL  - 5
DO  - 10.1038/srep15772
ER  - 

@article{
author = "Lončar, Nikola L. and Šokarda-Slavić, Marinela and Vujčić, Zoran and Božić, Nataša",
year = "2015",
abstract = "Bacillus licheniformis 9945a alpha-amylase is known as a potent enzyme for raw starch hydrolysis. In this paper, a mixed mode Nuvia cPrime (TM) resin is examined with the aim to improve the downstream processing of raw starch digesting amylases and exploit the hydrophobic patches on their surface. This resin combines hydrophobic interactions with cation exchange groups and as such the presence of salt facilitates hydrophobic interactions while the ion-exchange groups enable proper selectivity. alpha-Amylase was produced using an optimized fed-batch approach in a defined media and significant overexpression of 1.2 g L-1 was achieved. This single step procedure enables simultaneous concentration, pigment removal as well as purification of amylase with yields of 96% directly from the fermentation broth.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases",
volume = "5",
doi = "10.1038/srep15772"
}

Lončar, N. L., Šokarda-Slavić, M., Vujčić, Z.,& Božić, N.. (2015). Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases. in Scientific Reports
Nature Publishing Group, London., 5.
https://doi.org/10.1038/srep15772

Lončar NL, Šokarda-Slavić M, Vujčić Z, Božić N. Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases. in Scientific Reports. 2015;5.
doi:10.1038/srep15772 .

Lončar, Nikola L., Šokarda-Slavić, Marinela, Vujčić, Zoran, Božić, Nataša, "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases" in Scientific Reports, 5 (2015),
https://doi.org/10.1038/srep15772 . .

TY  - DATA
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3384
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3384
ER  - 

@misc{
author = "Lončar, Nikola L. and Šokarda-Slavić, Marinela and Vujčić, Zoran and Božić, Nataša",
year = "2015",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3384"
}

Lončar, N. L., Šokarda-Slavić, M., Vujčić, Z.,& Božić, N.. (2015). Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772. in Scientific Reports
Nature Publishing Group, London..
https://hdl.handle.net/21.15107/rcub_cherry_3384

Lončar NL, Šokarda-Slavić M, Vujčić Z, Božić N. Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772. in Scientific Reports. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3384 .

Lončar, Nikola L., Šokarda-Slavić, Marinela, Vujčić, Zoran, Božić, Nataša, "Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772" in Scientific Reports (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3384 .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Fraaije, Marco W.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1664
AB  - Thermobifida fusca is a mesothermophilic organism known for its ability to degrade plant biomass and other organics, and it was demonstrated that it represents a rich resource of genes encoding for potent enzymes for biocatalysis. The thermostable catalase from T. fusca has been cloned and overexpressed in Escherichia coli with a yield of 400 mg/L. Heat treatment of disrupted cells at 60 A degrees C for 1 h resulted in enzyme preparation of high purity; hence, no chromatography steps are needed for large-scale production. Except for catalyzing the dismutation of hydrogen peroxide, TfuCat was also found to catalyze oxidations of phenolic compounds. The catalase activity was comparable to other described catalases while peroxidase activity was quite remarkable with a k (obs) of nearly 1000 s(-1) for catechol. Site directed mutagenesis was used to alter the ratio of peroxidase/catalase activity. Resistance to inhibition by classic catalase inhibitors and an apparent melting temperature of 74 A degrees C classifies this enzyme as a robust biocatalyst. As such, it could compete with other commercially available catalases while the relatively high peroxidase activity also offers new biocatalytic possibilities.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity
VL  - 99
IS  - 5
SP  - 2225
EP  - 2232
DO  - 10.1007/s00253-014-6060-5
ER  - 

@article{
author = "Lončar, Nikola L. and Fraaije, Marco W.",
year = "2015",
abstract = "Thermobifida fusca is a mesothermophilic organism known for its ability to degrade plant biomass and other organics, and it was demonstrated that it represents a rich resource of genes encoding for potent enzymes for biocatalysis. The thermostable catalase from T. fusca has been cloned and overexpressed in Escherichia coli with a yield of 400 mg/L. Heat treatment of disrupted cells at 60 A degrees C for 1 h resulted in enzyme preparation of high purity; hence, no chromatography steps are needed for large-scale production. Except for catalyzing the dismutation of hydrogen peroxide, TfuCat was also found to catalyze oxidations of phenolic compounds. The catalase activity was comparable to other described catalases while peroxidase activity was quite remarkable with a k (obs) of nearly 1000 s(-1) for catechol. Site directed mutagenesis was used to alter the ratio of peroxidase/catalase activity. Resistance to inhibition by classic catalase inhibitors and an apparent melting temperature of 74 A degrees C classifies this enzyme as a robust biocatalyst. As such, it could compete with other commercially available catalases while the relatively high peroxidase activity also offers new biocatalytic possibilities.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity",
volume = "99",
number = "5",
pages = "2225-2232",
doi = "10.1007/s00253-014-6060-5"
}

Lončar, N. L.,& Fraaije, M. W.. (2015). Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity. in Applied Microbiology and Biotechnology
Springer, New York., 99(5), 2225-2232.
https://doi.org/10.1007/s00253-014-6060-5

Lončar NL, Fraaije MW. Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity. in Applied Microbiology and Biotechnology. 2015;99(5):2225-2232.
doi:10.1007/s00253-014-6060-5 .

Lončar, Nikola L., Fraaije, Marco W., "Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity" in Applied Microbiology and Biotechnology, 99, no. 5 (2015):2225-2232,
https://doi.org/10.1007/s00253-014-6060-5 . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Fraaije, Marco W.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1682
AB  - Catalases represent a class of enzymes which has found its place among industrially relevant biocatalysts due to their exceptional catalytic rate and high stability. Textile bleaching prior to the dyeing process is the main application and has been performed on a large scale for the past few decades. Their limited substrate scope has not prevented the development of various other catalase-based applications. Newly developed approaches continue to exploit their excellent catalytic potential to degrade hydrogen peroxide while (per)oxidase activity of catalases is opening a new range of possibilities as well. This review provides an overview of applications that involve heme-containing catalases that have been demonstrated in recent years.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Catalases as biocatalysts in technical applications: current state and perspectives
VL  - 99
IS  - 8
SP  - 3351
EP  - 3357
DO  - 10.1007/s00253-015-6512-6
ER  - 

@article{
author = "Lončar, Nikola L. and Fraaije, Marco W.",
year = "2015",
abstract = "Catalases represent a class of enzymes which has found its place among industrially relevant biocatalysts due to their exceptional catalytic rate and high stability. Textile bleaching prior to the dyeing process is the main application and has been performed on a large scale for the past few decades. Their limited substrate scope has not prevented the development of various other catalase-based applications. Newly developed approaches continue to exploit their excellent catalytic potential to degrade hydrogen peroxide while (per)oxidase activity of catalases is opening a new range of possibilities as well. This review provides an overview of applications that involve heme-containing catalases that have been demonstrated in recent years.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Catalases as biocatalysts in technical applications: current state and perspectives",
volume = "99",
number = "8",
pages = "3351-3357",
doi = "10.1007/s00253-015-6512-6"
}

Lončar, N. L.,& Fraaije, M. W.. (2015). Catalases as biocatalysts in technical applications: current state and perspectives. in Applied Microbiology and Biotechnology
Springer, New York., 99(8), 3351-3357.
https://doi.org/10.1007/s00253-015-6512-6

Lončar NL, Fraaije MW. Catalases as biocatalysts in technical applications: current state and perspectives. in Applied Microbiology and Biotechnology. 2015;99(8):3351-3357.
doi:10.1007/s00253-015-6512-6 .

Lončar, Nikola L., Fraaije, Marco W., "Catalases as biocatalysts in technical applications: current state and perspectives" in Applied Microbiology and Biotechnology, 99, no. 8 (2015):3351-3357,
https://doi.org/10.1007/s00253-015-6512-6 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stevanović, Nikola R.
AU  - Lončar, Nikola L.
AU  - Baošić, Rada
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1771
AB  - Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia
VL  - 79
IS  - 4
SP  - 411
EP  - 420
DO  - 10.2298/JSC130909155G
ER  - 

@article{
author = "Gligorijević, Nikola and Stevanović, Nikola R. and Lončar, Nikola L. and Baošić, Rada and Vujčić, Zoran and Božić, Nataša",
year = "2014",
abstract = "Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia",
volume = "79",
number = "4",
pages = "411-420",
doi = "10.2298/JSC130909155G"
}

Gligorijević, N., Stevanović, N. R., Lončar, N. L., Baošić, R., Vujčić, Z.,& Božić, N.. (2014). A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 79(4), 411-420.
https://doi.org/10.2298/JSC130909155G

Gligorijević N, Stevanović NR, Lončar NL, Baošić R, Vujčić Z, Božić N. A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society. 2014;79(4):411-420.
doi:10.2298/JSC130909155G .

Gligorijević, Nikola, Stevanović, Nikola R., Lončar, Nikola L., Baošić, Rada, Vujčić, Zoran, Božić, Nataša, "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia" in Journal of the Serbian Chemical Society, 79, no. 4 (2014):411-420,
https://doi.org/10.2298/JSC130909155G . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Gligorijević, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1791
AB  - Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia
VL  - 91
SP  - 18
EP  - 23
DO  - 10.1016/j.ibiod.2014.03.008
ER  - 

@article{
author = "Lončar, Nikola L. and Gligorijević, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2014",
abstract = "Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia",
volume = "91",
pages = "18-23",
doi = "10.1016/j.ibiod.2014.03.008"
}

Lončar, N. L., Gligorijević, N., Božić, N.,& Vujčić, Z.. (2014). Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 91, 18-23.
https://doi.org/10.1016/j.ibiod.2014.03.008

Lončar NL, Gligorijević N, Božić N, Vujčić Z. Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation. 2014;91:18-23.
doi:10.1016/j.ibiod.2014.03.008 .

Lončar, Nikola L., Gligorijević, Nikola, Božić, Nataša, Vujčić, Zoran, "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia" in International Biodeterioration and Biodegradation, 91 (2014):18-23,
https://doi.org/10.1016/j.ibiod.2014.03.008 . .

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1844
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
ER  - 

@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025"
}

Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025

Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025 .

Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 . .

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3743
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
ER  - 

@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025"
}

Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025

Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025 .

Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 . .

TY  - JOUR
AU  - Ćilerdžić, Jasmina
AU  - Stajić, Mirjana
AU  - Vukojević, Jelena
AU  - Lončar, Nikola L.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1872
AB  - Ganoderma lucidum has a well-developed ligninolytic enzyme system, where laccase is the dominant and sometimes only synthesizing enzyme, and therefore could find an application in the delignification of abundant plant raw materials and in food, feed, paper, and biofuel production. The questions that provided the goals for the present study were whether the profile of G. lucidum laccase depends on cultivation type and carbon source, as well as whether intraspecific diversity exists. Conditions of submerged cultivation proved more preferable for laccase activity compared with solid-state cultivations in all studied strains, while oak sawdust provided a better carbon source than wheat straw. Maximum laccase activity (7241.0 U/L) was measured on day 14 of oak sawdust submerged fermentation by strain BEOFB 431. Intraspecific diversity in synthesized proteins was more significant in wheat straw than in oak sawdust submerged fermentation. The profile of laccase isoforms was dependent on strain, plant residue, type, and period of cultivation. Four acidic laccase isoforms (pl 3.6) were detected in G. lucidum BEOFB 431 at the same cultivation point where maximal enzyme activity was measured.
PB  - North Carolina State Univ Dept Wood & Paper Sci, Raleigh
T2  - BioResources
T1  - Intraspecific Diversity in the Production and Characterization of Laccase within Ganoderma lucidum
VL  - 9
IS  - 3
SP  - 5577
EP  - 5587
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1872
ER  - 

@article{
author = "Ćilerdžić, Jasmina and Stajić, Mirjana and Vukojević, Jelena and Lončar, Nikola L.",
year = "2014",
abstract = "Ganoderma lucidum has a well-developed ligninolytic enzyme system, where laccase is the dominant and sometimes only synthesizing enzyme, and therefore could find an application in the delignification of abundant plant raw materials and in food, feed, paper, and biofuel production. The questions that provided the goals for the present study were whether the profile of G. lucidum laccase depends on cultivation type and carbon source, as well as whether intraspecific diversity exists. Conditions of submerged cultivation proved more preferable for laccase activity compared with solid-state cultivations in all studied strains, while oak sawdust provided a better carbon source than wheat straw. Maximum laccase activity (7241.0 U/L) was measured on day 14 of oak sawdust submerged fermentation by strain BEOFB 431. Intraspecific diversity in synthesized proteins was more significant in wheat straw than in oak sawdust submerged fermentation. The profile of laccase isoforms was dependent on strain, plant residue, type, and period of cultivation. Four acidic laccase isoforms (pl 3.6) were detected in G. lucidum BEOFB 431 at the same cultivation point where maximal enzyme activity was measured.",
publisher = "North Carolina State Univ Dept Wood & Paper Sci, Raleigh",
journal = "BioResources",
title = "Intraspecific Diversity in the Production and Characterization of Laccase within Ganoderma lucidum",
volume = "9",
number = "3",
pages = "5577-5587",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1872"
}

Ćilerdžić, J., Stajić, M., Vukojević, J.,& Lončar, N. L.. (2014). Intraspecific Diversity in the Production and Characterization of Laccase within Ganoderma lucidum. in BioResources
North Carolina State Univ Dept Wood & Paper Sci, Raleigh., 9(3), 5577-5587.
https://hdl.handle.net/21.15107/rcub_cherry_1872

Ćilerdžić J, Stajić M, Vukojević J, Lončar NL. Intraspecific Diversity in the Production and Characterization of Laccase within Ganoderma lucidum. in BioResources. 2014;9(3):5577-5587.
https://hdl.handle.net/21.15107/rcub_cherry_1872 .

Ćilerdžić, Jasmina, Stajić, Mirjana, Vukojević, Jelena, Lončar, Nikola L., "Intraspecific Diversity in the Production and Characterization of Laccase within Ganoderma lucidum" in BioResources, 9, no. 3 (2014):5577-5587,
https://hdl.handle.net/21.15107/rcub_cherry_1872 .

TY  - CONF
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1420
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1
VL  - 280
SP  - 599
EP  - 599
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1420
ER  - 

@conference{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1",
volume = "280",
pages = "599-599",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1420"
}

Lončar, N. L., Božić, N.,& Vujčić, Z.. (2013). Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 599-599.
https://hdl.handle.net/21.15107/rcub_cherry_1420

Lončar NL, Božić N, Vujčić Z. Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1. in FEBS Journal / Federation of European of Biochemical Societies. 2013;280:599-599.
https://hdl.handle.net/21.15107/rcub_cherry_1420 .

Lončar, Nikola L., Božić, Nataša, Vujčić, Zoran, "Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1" in FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):599-599,
https://hdl.handle.net/21.15107/rcub_cherry_1420 .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1431
AB  - One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization
VL  - 147
SP  - 177
EP  - 183
DO  - 10.1016/j.biortech.2013.08.056
ER  - 

@article{
author = "Lončar, Nikola L. and Božić, Nataša and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization",
volume = "147",
pages = "177-183",
doi = "10.1016/j.biortech.2013.08.056"
}

Lončar, N. L., Božić, N., Lopez-Santin, J.,& Vujčić, Z.. (2013). Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 147, 177-183.
https://doi.org/10.1016/j.biortech.2013.08.056

Lončar NL, Božić N, Lopez-Santin J, Vujčić Z. Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology. 2013;147:177-183.
doi:10.1016/j.biortech.2013.08.056 .

Lončar, Nikola L., Božić, Nataša, Lopez-Santin, Josep, Vujčić, Zoran, "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization" in Bioresource Technology, 147 (2013):177-183,
https://doi.org/10.1016/j.biortech.2013.08.056 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Puertas, Juan-Miguel
AU  - Lončar, Nikola L.
AU  - Sans Duran, Cristina
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1638
AB  - In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a
VL  - 48
IS  - 3
SP  - 438
EP  - 442
DO  - 10.1016/j.procbio.2013.01.016
ER  - 

@article{
author = "Božić, Nataša and Puertas, Juan-Miguel and Lončar, Nikola L. and Sans Duran, Cristina and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a",
volume = "48",
number = "3",
pages = "438-442",
doi = "10.1016/j.procbio.2013.01.016"
}

Božić, N., Puertas, J., Lončar, N. L., Sans Duran, C., Lopez-Santin, J.,& Vujčić, Z.. (2013). The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 48(3), 438-442.
https://doi.org/10.1016/j.procbio.2013.01.016

Božić N, Puertas J, Lončar NL, Sans Duran C, Lopez-Santin J, Vujčić Z. The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry. 2013;48(3):438-442.
doi:10.1016/j.procbio.2013.01.016 .

Božić, Nataša, Puertas, Juan-Miguel, Lončar, Nikola L., Sans Duran, Cristina, Lopez-Santin, Josep, Vujčić, Zoran, "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a" in Process Biochemistry, 48, no. 3 (2013):438-442,
https://doi.org/10.1016/j.procbio.2013.01.016 . .

TY  - JOUR
AU  - Knežević, Aleksandar
AU  - Milovanović, Ivan
AU  - Stajić, Mirjana
AU  - Lončar, Nikola L.
AU  - Brčeski, Ilija
AU  - Vukojević, Jelena
AU  - Ćilerdžić, Jasmina
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1364
AB  - As biological decomposition of plant biomass represents a popular alternative environmental-friendly and economically justified process, screening of ligninolytic enzyme systems of various fungal species is a topical study area. The goal of the study was to obtain clear insight into the dynamics of laccase, Mn-dependent peroxidase, and Mn-independent peroxidase activity and levels of wheat straw lignin degradation in seven wood-rotting fungi. The best laccase producers were Pleurotus ostreatus and Pleurotus eryngii. Lenzites betulinus and Fomitopsis pinicola were the best Mn-dependent peroxidase producers, and P. ostreatus the weakest one. The peak of Mn-independent peroxidase was noted in Dichomytus squalens, and the minimum value in P. ostreatus. The profiles of the three enzymes, obtained by isoelectric focusing, were variable depending on the species and cultivation period. D. squalens was the best lignin degrader (34.1% of total lignin amount), and P. ostreatus and P. eryngii the weakest ones (7.1% and 14.5%, respectively).
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Lignin degradation by selected fungal species
VL  - 138
SP  - 117
EP  - 123
DO  - 10.1016/j.biortech.2013.03.182
ER  - 

@article{
author = "Knežević, Aleksandar and Milovanović, Ivan and Stajić, Mirjana and Lončar, Nikola L. and Brčeski, Ilija and Vukojević, Jelena and Ćilerdžić, Jasmina",
year = "2013",
abstract = "As biological decomposition of plant biomass represents a popular alternative environmental-friendly and economically justified process, screening of ligninolytic enzyme systems of various fungal species is a topical study area. The goal of the study was to obtain clear insight into the dynamics of laccase, Mn-dependent peroxidase, and Mn-independent peroxidase activity and levels of wheat straw lignin degradation in seven wood-rotting fungi. The best laccase producers were Pleurotus ostreatus and Pleurotus eryngii. Lenzites betulinus and Fomitopsis pinicola were the best Mn-dependent peroxidase producers, and P. ostreatus the weakest one. The peak of Mn-independent peroxidase was noted in Dichomytus squalens, and the minimum value in P. ostreatus. The profiles of the three enzymes, obtained by isoelectric focusing, were variable depending on the species and cultivation period. D. squalens was the best lignin degrader (34.1% of total lignin amount), and P. ostreatus and P. eryngii the weakest ones (7.1% and 14.5%, respectively).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Lignin degradation by selected fungal species",
volume = "138",
pages = "117-123",
doi = "10.1016/j.biortech.2013.03.182"
}

Knežević, A., Milovanović, I., Stajić, M., Lončar, N. L., Brčeski, I., Vukojević, J.,& Ćilerdžić, J.. (2013). Lignin degradation by selected fungal species. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 138, 117-123.
https://doi.org/10.1016/j.biortech.2013.03.182

Knežević A, Milovanović I, Stajić M, Lončar NL, Brčeski I, Vukojević J, Ćilerdžić J. Lignin degradation by selected fungal species. in Bioresource Technology. 2013;138:117-123.
doi:10.1016/j.biortech.2013.03.182 .

Knežević, Aleksandar, Milovanović, Ivan, Stajić, Mirjana, Lončar, Nikola L., Brčeski, Ilija, Vukojević, Jelena, Ćilerdžić, Jasmina, "Lignin degradation by selected fungal species" in Bioresource Technology, 138 (2013):117-123,
https://doi.org/10.1016/j.biortech.2013.03.182 . .

TY  - THES
AU  - Lončar, Nikola L.
PY  - 2012
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=236
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:5503/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=43576847
UR  - http://nardus.mpn.gov.rs/123456789/3460
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2604
AB  - Boje i halogenovani fenoli koji imaju dezaktivirano aromatiĉno jezgro ĉineznaĉajnu kategoriju veoma toksiĉnih i teško razgradljivih zagaĊivaĉa u raznimindustrijskim granama. Glavni cilj ove disertacije je bio dobivanje jeftinih rastvornih iimobilizovanih enzima za uklanjanje fenola i boja iz otpadnih voda. Korišćeno je ĉetiriprirodna (nativna) enzima (polifenoloksidaza iz krompira, tri lakaze na sporamaizolovanih sojeva Bacillus amyloliquefaciens, lakaza iz gljive Trametes versicolor,kisele i bazne izoforme peroksidaze iz rena) i dva rekombinantna enzima(hloroperoksidaza iz Caldariomyces fumago proizvedena u Aspergillus niger i lakaza izsoja B. amyloliquefaciens 12B1 proizvedena u Escherichia coli).Djelimiĉno preĉišćena polifenoloksidaza (PPO) iz krompira je imobilizovana narazliĉitim nosaĉima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO,Eupergit C250L-PPO, Celit-PPO i CelulozaM-PPO, su testirani u reaktoru za uklanjanjefenola, p-hlorfenola i p-bromfenola. U sluĉaju 2,5 mM supstrata sa Eupergit C250LPPO,postignuto je oko 45% razgradnje p-bromfenola, dok su p-hlorfenol i fenolrazgraĊeni 35% odnosno 20%. Testirana je i sposobnost višestruke upotrebe EupergitC250L-PPO imobilizata za uklanjanje p-hlorfenola. Iz eksperimenata sinteze novognosaĉa sa pipcima i njegove primjene za imobilizaciju PPO može se zakljuĉiti da jeimobilizovana PPO bila znatno otpornija na denaturaciju u odnosu na solubilni enzim.Biokatalizator je testiran u šaržnom reaktoru za uklanjanje p-hlorfenola i p-bromfenolaiz vodenih rastvora. Postignuto je uklanjanje pomenutih fenola preko 90% prikoncentraciji fenola 100 mg/L. Za oba halogenfenola TC-PPO je pokazao stepenuklanjanja od preko 90% u prva tri ciklusa, nakon ĉega efikasnost opada do 60% nakonšest ciklusa od po 8 ĉasova. Rastvornom PPO pod optimizovanim uslovima moguće jeukloniti 93-99.9% boje nakon tretmana u trajanju od 1 ĉas sa 424-1700 U/mL PPO,zavisno od boje. Pokazano je da je optimalno pH za proces obezbojavanja bilo 3,0.Obezbojavanje je postignuto uz formiranje nerastvornih polimera koji su uklonjenifiltrovanjem ili centrifugiranjem. Formiranje polimera potvrĊeno je infracrvenomspektroskopijom...
AB  - Dyes and phenols containing halogens which tend to deactivate the aromaticnuclei constitute a significant category of highly toxic and difficult-to-degradepollutants from a wide variety of industries. Main goal of this dissertation was theproduction of inexpensive soluble and immobilized enzymes for removal of phenols anddyes from wastewater. Four native enzymes (potato polyphenoloxidase, three laccaseson spores of isolated strains of Bacillus amyloliquefaciens, laccase from Trametesversicolor, acidic and basic isoforms of horseradish peroxidase) and two recombinantenzymes (chloroperoxidase from Caldariomyces fumago produced in Aspergillus nigerand laccase from B. amyloliquefaciens 12B1 strain produced in Escherichia coli).Partially purified potato polyphenol oxidase (PPO) was immobilized ontodifferent commercial and laboratory produced carriers. The three of the obtainedbiocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO, Celite-PPOand CelluloseM-PPO, were tested in the batch reactor for phenol, p-chlorophenol and pbromophenolremoval. In the case of 2.5 mM substrates with Eupergit C250L-PPO,around 45% removal of p-bromophenol was achieved, while p-chlorophenol and phenolwere removed 35% and 20%, respectively. The reusability of Eupergit C250L-PPO forthe removal of p-chlorophenol has been tested. From experiments of synthesis of newtentacle carrier and its application for PPO immobilization we can conclude thatimmobilized PPO was more resistant to denaturation when compared with its solublecounterpart. Biocatalyst was tested in the batch reactor for p-chlorophenol and pbromophenolremoval from aqueous solution. More than 90% removal was achieved forboth halogenophenols at concentration of 100 mg/l from aqueous solution. For bothhalogenophenols TC-PPO works with over 90% removal during first three cycles whichdecrease to 60% removal efficiency after six cycles each of 8 hours duration. Withsoluble PPO, under optimized conditions 93-99.9% removal of dyes was achieved after1h using 424 – 1700 U/mL of PPO, depending on dye. Optimum pH for decolorizationprocess was found to be 3.0. Decolorization was accomplished via insoluble polymersformations that were separated by filtration or centrifugation. Polymer formation wasconfirmed with infrared spectroscopy...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Uklanjanje fenola i boja iz otpadne vode prirodnim i rekombinantnim oksidativnim enzimima
T1  - Removal of phenols and dyes from wastewater using native and recombinant oxidative enzymes
UR  - https://hdl.handle.net/21.15107/rcub_nardus_3460
ER  - 

@phdthesis{
author = "Lončar, Nikola L.",
year = "2012",
abstract = "Boje i halogenovani fenoli koji imaju dezaktivirano aromatiĉno jezgro ĉineznaĉajnu kategoriju veoma toksiĉnih i teško razgradljivih zagaĊivaĉa u raznimindustrijskim granama. Glavni cilj ove disertacije je bio dobivanje jeftinih rastvornih iimobilizovanih enzima za uklanjanje fenola i boja iz otpadnih voda. Korišćeno je ĉetiriprirodna (nativna) enzima (polifenoloksidaza iz krompira, tri lakaze na sporamaizolovanih sojeva Bacillus amyloliquefaciens, lakaza iz gljive Trametes versicolor,kisele i bazne izoforme peroksidaze iz rena) i dva rekombinantna enzima(hloroperoksidaza iz Caldariomyces fumago proizvedena u Aspergillus niger i lakaza izsoja B. amyloliquefaciens 12B1 proizvedena u Escherichia coli).Djelimiĉno preĉišćena polifenoloksidaza (PPO) iz krompira je imobilizovana narazliĉitim nosaĉima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO,Eupergit C250L-PPO, Celit-PPO i CelulozaM-PPO, su testirani u reaktoru za uklanjanjefenola, p-hlorfenola i p-bromfenola. U sluĉaju 2,5 mM supstrata sa Eupergit C250LPPO,postignuto je oko 45% razgradnje p-bromfenola, dok su p-hlorfenol i fenolrazgraĊeni 35% odnosno 20%. Testirana je i sposobnost višestruke upotrebe EupergitC250L-PPO imobilizata za uklanjanje p-hlorfenola. Iz eksperimenata sinteze novognosaĉa sa pipcima i njegove primjene za imobilizaciju PPO može se zakljuĉiti da jeimobilizovana PPO bila znatno otpornija na denaturaciju u odnosu na solubilni enzim.Biokatalizator je testiran u šaržnom reaktoru za uklanjanje p-hlorfenola i p-bromfenolaiz vodenih rastvora. Postignuto je uklanjanje pomenutih fenola preko 90% prikoncentraciji fenola 100 mg/L. Za oba halogenfenola TC-PPO je pokazao stepenuklanjanja od preko 90% u prva tri ciklusa, nakon ĉega efikasnost opada do 60% nakonšest ciklusa od po 8 ĉasova. Rastvornom PPO pod optimizovanim uslovima moguće jeukloniti 93-99.9% boje nakon tretmana u trajanju od 1 ĉas sa 424-1700 U/mL PPO,zavisno od boje. Pokazano je da je optimalno pH za proces obezbojavanja bilo 3,0.Obezbojavanje je postignuto uz formiranje nerastvornih polimera koji su uklonjenifiltrovanjem ili centrifugiranjem. Formiranje polimera potvrĊeno je infracrvenomspektroskopijom..., Dyes and phenols containing halogens which tend to deactivate the aromaticnuclei constitute a significant category of highly toxic and difficult-to-degradepollutants from a wide variety of industries. Main goal of this dissertation was theproduction of inexpensive soluble and immobilized enzymes for removal of phenols anddyes from wastewater. Four native enzymes (potato polyphenoloxidase, three laccaseson spores of isolated strains of Bacillus amyloliquefaciens, laccase from Trametesversicolor, acidic and basic isoforms of horseradish peroxidase) and two recombinantenzymes (chloroperoxidase from Caldariomyces fumago produced in Aspergillus nigerand laccase from B. amyloliquefaciens 12B1 strain produced in Escherichia coli).Partially purified potato polyphenol oxidase (PPO) was immobilized ontodifferent commercial and laboratory produced carriers. The three of the obtainedbiocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO, Celite-PPOand CelluloseM-PPO, were tested in the batch reactor for phenol, p-chlorophenol and pbromophenolremoval. In the case of 2.5 mM substrates with Eupergit C250L-PPO,around 45% removal of p-bromophenol was achieved, while p-chlorophenol and phenolwere removed 35% and 20%, respectively. The reusability of Eupergit C250L-PPO forthe removal of p-chlorophenol has been tested. From experiments of synthesis of newtentacle carrier and its application for PPO immobilization we can conclude thatimmobilized PPO was more resistant to denaturation when compared with its solublecounterpart. Biocatalyst was tested in the batch reactor for p-chlorophenol and pbromophenolremoval from aqueous solution. More than 90% removal was achieved forboth halogenophenols at concentration of 100 mg/l from aqueous solution. For bothhalogenophenols TC-PPO works with over 90% removal during first three cycles whichdecrease to 60% removal efficiency after six cycles each of 8 hours duration. Withsoluble PPO, under optimized conditions 93-99.9% removal of dyes was achieved after1h using 424 – 1700 U/mL of PPO, depending on dye. Optimum pH for decolorizationprocess was found to be 3.0. Decolorization was accomplished via insoluble polymersformations that were separated by filtration or centrifugation. Polymer formation wasconfirmed with infrared spectroscopy...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Uklanjanje fenola i boja iz otpadne vode prirodnim i rekombinantnim oksidativnim enzimima, Removal of phenols and dyes from wastewater using native and recombinant oxidative enzymes",
url = "https://hdl.handle.net/21.15107/rcub_nardus_3460"
}

Lončar, N. L.. (2012). Uklanjanje fenola i boja iz otpadne vode prirodnim i rekombinantnim oksidativnim enzimima. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_3460

Lončar NL. Uklanjanje fenola i boja iz otpadne vode prirodnim i rekombinantnim oksidativnim enzimima. in Универзитет у Београду. 2012;.
https://hdl.handle.net/21.15107/rcub_nardus_3460 .

Lončar, Nikola L., "Uklanjanje fenola i boja iz otpadne vode prirodnim i rekombinantnim oksidativnim enzimima" in Универзитет у Београду (2012),
https://hdl.handle.net/21.15107/rcub_nardus_3460 .