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

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

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

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

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

TY  - JOUR
AU  - Božić, Nataša
AU  - Rozeboom, Henriëtte J.
AU  - Lončar, Nikola
AU  - Šokarda Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3728
AB  - α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase
VL  - 165
IS  - A
SP  - 1529
EP  - 1539
DO  - 10.1016/j.ijbiomac.2020.10.025
ER  - 

@article{
author = "Božić, Nataša and Rozeboom, Henriëtte J. and Lončar, Nikola and Šokarda Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase",
volume = "165",
number = "A",
pages = "1529-1539",
doi = "10.1016/j.ijbiomac.2020.10.025"
}

Božić, N., Rozeboom, H. J., Lončar, N., Šokarda Slavić, M., Janssen, D. B.,& Vujčić, Z.. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. 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 N, 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, 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
AU  - Šokarda Slavić, Marinela
AU  - Janssen, Dick B.
AU  - Vujčić, Zoran
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3736
AB  - α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase
VL  - 165
IS  - A
SP  - 1529
EP  - 1539
DO  - 10.1016/j.ijbiomac.2020.10.025
ER  - 

@article{
author = "Božić, Nataša and Rozeboom, Henriëtte J. and Lončar, Nikola and Šokarda Slavić, Marinela and Janssen, Dick B. and Vujčić, Zoran",
year = "2020",
abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy), belonging to GH13_5 subfamily of glycoside hydrolases, was proven to be a highly efficient raw starch digesting enzyme. The ability of some α-amylases to hydrolyze raw starch is related to the existence of surface binding sites (SBSs) for polysaccharides that can be distant from the active site. Crystallographic studies performed on BliAmy in the apo form and of enzyme bound with different oligosaccharides and oligosaccharide precursors revealed binding of these ligands to one SBS with two amino acids F257 and Y358 mainly involved in complex formation. The role of this SBS in starch binding and degradation was probed by designing enzyme variants mutated in this region (F257A and Y358A). Kinetic studies with different substrates show that starch binding through the SBS is disrupted in the mutants and that F257 and Y358 contributed cumulatively to binding and hydrolysis. Mutation of both sites (F257A/Y358A) resulted in a 5-fold lower efficacy with raw starch as substrate and at least 5.5-fold weaker binding compared to the wild type BliAmy, suggesting that the ability of BliAmy to hydrolyze raw starch with high efficiency is related to the level of its adsorption onto starch granules.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase",
volume = "165",
number = "A",
pages = "1529-1539",
doi = "10.1016/j.ijbiomac.2020.10.025"
}

Božić, N., Rozeboom, H. J., Lončar, N., Šokarda Slavić, M., Janssen, D. B.,& Vujčić, Z.. (2020). Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase. 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 N, 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, 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
AU  - Drašković, Natalija
AU  - Božić, Nataša
AU  - Romero, Elvira
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Vujčić, Zoran
AU  - Fraaije, Marco W.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3021
AB  - The consumption of dyes is increasing worldwide in line with the increase of population
and demand for clothes and other colored products. However, the e ciency of dyeing processes
is still poor and results in large amounts of colored e uents. It is desired to develop a portfolio
of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome
sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (PfDyP B2) could be overexpressed as a soluble protein. PfDyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of PfDyP B2 in calcium-alginate beads resulted in a significant increase in stability: PfDyP B2 retains 80% of its initial activity after 2 h incubation at 50 °C, while the soluble enzyme is inactivated within minutes. PfDyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30 °C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.
PB  - MDPI
T2  - Catalysts
T1  - Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1
VL  - 9
SP  - 463
DO  - 10.3390/catal9050463
ER  - 

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

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

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

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

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

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

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

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

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

TY  - JOUR
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3131
AB  - Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications.
PB  - Elsevier
T2  - Journal of Molecular Catalysis B: Enzymatic
T1  - Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
VL  - 134
SP  - 390
EP  - 395
DO  - 10.1016/j.molcatb.2016.06.005
ER  - 

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

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

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

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

TY  - CONF
AU  - Šokarda Slavić, Marinela
AU  - Lončar, Nikola
AU  - Janeček, Štefan
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3551
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Sixth Conference, “Biochemistry and Interdisciplinarity: Transcending the Limits of Field”, Faculty of Chemistry, University of Belgrade, 18.11.2016. Belgrade, Serbia
T1  - Rational design of raw starch degrading α-amylase from Bacillus licheniformis 9945a for possible surface binding sites indetification
SP  - 159
EP  - 159
UR  - https://hdl.handle.net/21.15107/rcub_cer_3551
ER  - 

@conference{
author = "Šokarda Slavić, Marinela and Lončar, Nikola and Janeček, Štefan and Vujčić, Zoran and Božić, Nataša",
year = "2016",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Sixth Conference, “Biochemistry and Interdisciplinarity: Transcending the Limits of Field”, Faculty of Chemistry, University of Belgrade, 18.11.2016. Belgrade, Serbia",
title = "Rational design of raw starch degrading α-amylase from Bacillus licheniformis 9945a for possible surface binding sites indetification",
pages = "159-159",
url = "https://hdl.handle.net/21.15107/rcub_cer_3551"
}

Šokarda Slavić, M., Lončar, N., Janeček, Š., Vujčić, Z.,& Božić, N.. (2016). Rational design of raw starch degrading α-amylase from Bacillus licheniformis 9945a for possible surface binding sites indetification. in Serbian Biochemical Society Sixth Conference, “Biochemistry and Interdisciplinarity: Transcending the Limits of Field”, Faculty of Chemistry, University of Belgrade, 18.11.2016. Belgrade, Serbia
Serbian Biochemical Society., 159-159.
https://hdl.handle.net/21.15107/rcub_cer_3551

Šokarda Slavić M, Lončar N, Janeček Š, Vujčić Z, Božić N. Rational design of raw starch degrading α-amylase from Bacillus licheniformis 9945a for possible surface binding sites indetification. in Serbian Biochemical Society Sixth Conference, “Biochemistry and Interdisciplinarity: Transcending the Limits of Field”, Faculty of Chemistry, University of Belgrade, 18.11.2016. Belgrade, Serbia. 2016;:159-159.
https://hdl.handle.net/21.15107/rcub_cer_3551 .

Šokarda Slavić, Marinela, Lončar, Nikola, Janeček, Štefan, Vujčić, Zoran, Božić, Nataša, "Rational design of raw starch degrading α-amylase from Bacillus licheniformis 9945a for possible surface binding sites indetification" in Serbian Biochemical Society Sixth Conference, “Biochemistry and Interdisciplinarity: Transcending the Limits of Field”, Faculty of Chemistry, University of Belgrade, 18.11.2016. Belgrade, Serbia (2016):159-159,
https://hdl.handle.net/21.15107/rcub_cer_3551 .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Janović, Barbara
AU  - Lončar, Nikola
AU  - Margetić, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1760
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.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration & 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 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.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration & 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., Margetić, A., Božić, N., Dojnov, B.,& Vujčić, M.. (2015). Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration & Biodegradation
Elsevier Sci Ltd, Oxford., 97, 124-127.
https://doi.org/10.1016/j.ibiod.2014.10.007

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

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

TY  - JOUR
AU  - Lončar, Nikola
AU  - Šokarda Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1815
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 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., 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 N, 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, 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  - CONF
AU  - Šokarda Slavić, Marinela
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3547
AB  - Bacillus licheniformis 9945a α-amylase (BliAmy) has been described as potent enzyme for raw starch hydrolysis. Starch represents an inexpensive source for production of glucose, maltose syrups and fructose which are widely used in food industries. Regarding energy costs, effective utilization of natural resources and viscosity problems, direct hydrolysis of raw starch below the gelatinization temperature by using raw-starch-digesting enzymes, such as α-amylase is desirable. In spite of the extensive studies concerning the structure and thermal properties of B. licheniformis amylase and the numerous reports in the literature referring to the molecular mechanism of irreversible thermoinactivation, little attention has been paid to its enzymological characterisation. Detailed knowledge about subsite architecture of B. licheniformis amylase is scarce. No report on kinetics and mode of action of this industrially important enzyme can be found in the literature especially when raw starch is used as a substrate. For mechanistic studies enzyme preparations of high purity are required and improving downstream processing is very beneficial. BliAmy was produced using optimized fed-batch approach in defined media and significant overexpression of 1.2 g L-1 was achieved. These amylases have exposed tyrosine and tryptophan residues as part of their surface binding sites. Mixed mode Nuvia cPrime™ resin is tested as improvement
of the downstream processing of raw starch digesting amylases aiming at exploiting hydrophobic patches at their surface. This resin combines hydrophobic interactions with cation exchange groups. Presence of salt facilitates hydrophobic interactions while ionexchange groups enable proper selectivity. Surface response methodology was used to optimize binding and eluting conditions of BliAmy. This single step procedure enables simultaneous concentration, pigments removal and purification of amylase with a yield of 96% directly from fermentation broth.
PB  - Serbian Biochemical Society (Belgrade)
C3  - Serbian Biochemical Society Fifth Conference, “Integrated research in life science”, Faculty of Chemistry, University of Belgrade, 13.11.2015. Belgrade, Serbia
T1  - Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases
SP  - 137
EP  - 137
UR  - https://hdl.handle.net/21.15107/rcub_cer_3547
ER  - 

@conference{
author = "Šokarda Slavić, Marinela and Lončar, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2015",
abstract = "Bacillus licheniformis 9945a α-amylase (BliAmy) has been described as potent enzyme for raw starch hydrolysis. Starch represents an inexpensive source for production of glucose, maltose syrups and fructose which are widely used in food industries. Regarding energy costs, effective utilization of natural resources and viscosity problems, direct hydrolysis of raw starch below the gelatinization temperature by using raw-starch-digesting enzymes, such as α-amylase is desirable. In spite of the extensive studies concerning the structure and thermal properties of B. licheniformis amylase and the numerous reports in the literature referring to the molecular mechanism of irreversible thermoinactivation, little attention has been paid to its enzymological characterisation. Detailed knowledge about subsite architecture of B. licheniformis amylase is scarce. No report on kinetics and mode of action of this industrially important enzyme can be found in the literature especially when raw starch is used as a substrate. For mechanistic studies enzyme preparations of high purity are required and improving downstream processing is very beneficial. BliAmy was produced using optimized fed-batch approach in defined media and significant overexpression of 1.2 g L-1 was achieved. These amylases have exposed tyrosine and tryptophan residues as part of their surface binding sites. Mixed mode Nuvia cPrime™ resin is tested as improvement
of the downstream processing of raw starch digesting amylases aiming at exploiting hydrophobic patches at their surface. This resin combines hydrophobic interactions with cation exchange groups. Presence of salt facilitates hydrophobic interactions while ionexchange groups enable proper selectivity. Surface response methodology was used to optimize binding and eluting conditions of BliAmy. This single step procedure enables simultaneous concentration, pigments removal and purification of amylase with a yield of 96% directly from fermentation broth.",
publisher = "Serbian Biochemical Society (Belgrade)",
journal = "Serbian Biochemical Society Fifth Conference, “Integrated research in life science”, Faculty of Chemistry, University of Belgrade, 13.11.2015. Belgrade, Serbia",
title = "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases",
pages = "137-137",
url = "https://hdl.handle.net/21.15107/rcub_cer_3547"
}

Šokarda Slavić, M., Lončar, N., Božić, N.,& Vujčić, Z.. (2015). Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases. in Serbian Biochemical Society Fifth Conference, “Integrated research in life science”, Faculty of Chemistry, University of Belgrade, 13.11.2015. Belgrade, Serbia
Serbian Biochemical Society (Belgrade)., 137-137.
https://hdl.handle.net/21.15107/rcub_cer_3547

Šokarda Slavić M, Lončar N, Božić N, Vujčić Z. Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases. in Serbian Biochemical Society Fifth Conference, “Integrated research in life science”, Faculty of Chemistry, University of Belgrade, 13.11.2015. Belgrade, Serbia. 2015;:137-137.
https://hdl.handle.net/21.15107/rcub_cer_3547 .

Šokarda Slavić, Marinela, Lončar, Nikola, Božić, Nataša, Vujčić, Zoran, "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases" in Serbian Biochemical Society Fifth Conference, “Integrated research in life science”, Faculty of Chemistry, University of Belgrade, 13.11.2015. Belgrade, Serbia (2015):137-137,
https://hdl.handle.net/21.15107/rcub_cer_3547 .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stevanovic, Nikola
AU  - Lončar, Nikola
AU  - Baošić, Rada
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1572
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 Stevanovic, Nikola and Lončar, Nikola 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., Stevanovic, N., Lončar, N., 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, Stevanovic N, Lončar N, 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, Stevanovic, Nikola, Lončar, Nikola, 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
AU  - Gligorijević, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1595
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.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration & 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 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.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration & 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., Gligorijević, N., Božić, N.,& Vujčić, Z.. (2014). Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration & Biodegradation
Elsevier Sci Ltd, Oxford., 91, 18-23.
https://doi.org/10.1016/j.ibiod.2014.03.008

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

Lončar, Nikola, Gligorijević, Nikola, Božić, Nataša, Vujčić, Zoran, "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia" in International Biodeterioration & 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
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3162
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.
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 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.",
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., 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 N, 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, 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
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1428
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.
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 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.",
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., 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 N, 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, 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  - Božić, Nataša
AU  - Puertas, Juan-Miguel
AU  - Lončar, Nikola
AU  - Sans, Duran Cristina
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1368
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.
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 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.",
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., Sans, D. 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 N, Sans DC, 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, 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  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1256
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.
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 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.",
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., 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 N, 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, 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  - CONF
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1174
UR  - https://doi.org/10.1111/febs.12340
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal
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 and Božić, Nataša and Vujčić, Zoran",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal",
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., Božić, N.,& Vujčić, Z.. (2013). Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1. in FEBS Journal
Wiley-Blackwell, Hoboken., 280, 599-599.
https://hdl.handle.net/21.15107/rcub_cherry_1420

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

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

TY  - JOUR
AU  - Lončar, Nikola
AU  - Janović, Barbara
AU  - Vujčić, Miroslava
AU  - Vujčić, Zoran
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1115
AB  - Potatoes are desirable source for polyphenol oxidase (PPO, EC 1.14.18.1) purification because this enzyme can be purified from the food industry waste such are potato peels from potato chips industry. This paper presents data concerning decolorization of 7 different, so far untested textile dyes and 3 real samples (industry effluents) by a partially purified PPO. Under optimized conditions 93-99.9% removal of dyes was achieved after 1 h using 424-1700 U ml(-1) of PPO, depending on dye. Optimum pH for decolorization process of all dyes was found to be 3.0. Potato PPO was capable of removing reactive dyes and textile dye effluents without requiring any mediator. Decolorization was accomplished via insoluble polymers formations that were separated by filtration.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration & Biodegradation
T1  - Decolorization of textile dyes and effluents using potato (Solanum tuberosum) phenoloxidase
VL  - 72
SP  - 42
EP  - 45
DO  - 10.1016/j.ibiod.2012.05.001
ER  - 

@article{
author = "Lončar, Nikola and Janović, Barbara and Vujčić, Miroslava and Vujčić, Zoran",
year = "2012",
abstract = "Potatoes are desirable source for polyphenol oxidase (PPO, EC 1.14.18.1) purification because this enzyme can be purified from the food industry waste such are potato peels from potato chips industry. This paper presents data concerning decolorization of 7 different, so far untested textile dyes and 3 real samples (industry effluents) by a partially purified PPO. Under optimized conditions 93-99.9% removal of dyes was achieved after 1 h using 424-1700 U ml(-1) of PPO, depending on dye. Optimum pH for decolorization process of all dyes was found to be 3.0. Potato PPO was capable of removing reactive dyes and textile dye effluents without requiring any mediator. Decolorization was accomplished via insoluble polymers formations that were separated by filtration.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration & Biodegradation",
title = "Decolorization of textile dyes and effluents using potato (Solanum tuberosum) phenoloxidase",
volume = "72",
pages = "42-45",
doi = "10.1016/j.ibiod.2012.05.001"
}

Lončar, N., Janović, B., Vujčić, M.,& Vujčić, Z.. (2012). Decolorization of textile dyes and effluents using potato (Solanum tuberosum) phenoloxidase. in International Biodeterioration & Biodegradation
Elsevier Sci Ltd, Oxford., 72, 42-45.
https://doi.org/10.1016/j.ibiod.2012.05.001

Lončar N, Janović B, Vujčić M, Vujčić Z. Decolorization of textile dyes and effluents using potato (Solanum tuberosum) phenoloxidase. in International Biodeterioration & Biodegradation. 2012;72:42-45.
doi:10.1016/j.ibiod.2012.05.001 .

Lončar, Nikola, Janović, Barbara, Vujčić, Miroslava, Vujčić, Zoran, "Decolorization of textile dyes and effluents using potato (Solanum tuberosum) phenoloxidase" in International Biodeterioration & Biodegradation, 72 (2012):42-45,
https://doi.org/10.1016/j.ibiod.2012.05.001 . .

TY  - JOUR
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Anđelković, Ivan
AU  - Milovanović, Aleksandra
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Roglić, Goran
AU  - Vujčić, Zoran
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/885
AB  - Phenols containing halogens, which tend to deactivate the aromatic nuclei, constitute a significant category of highly toxic and difficult-to-degrade pollutants, which arise from a wide variety of industries. The main purpose of this study was to obtain an inexpensive immobilized enzyme for the removal of phenols. Partially purified potato polyphenol oxidase (PPO) was immobilized onto different commercial and laboratory produced carriers. Three of the obtained biocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO; Celite-PPO and CelluloseM-PPO, were tested in a batch reactor for the removal of phenol, 4-chlorophenol and 4-bromophenol. In the case of 2.5 mM substrates with Eupergit C250L-PPO, an around 45% removal of 4-bromophenol was achieved, while the removals 4-chlorophenol and phenol were 35 and 20%, respectively. The reusability of Eupergit C250L-PPO for the removal of 4-chlorophenol was tested. After eight repeated tests, the efficiency of 4-chlorophenol removal by Eupergit C250L-PPO immobilisate had decreased to 55%.
AB  - Halogenovani fenoli imaju dezaktivirano aromatično jezgro i čine značajnu kategoriju veoma toksičnih i teško razgradivih zagađivača u raznim industrijskim granama. Glavni cilj ovog rada je bio dobijanje jeftinog imobilizovanog enzima za uklanjanje fenola. Delimično prečišćena polifenol-oksidaza (PFO) iz krompira je imobilizovana na različitim komercijalnim i laboratorijski sintetizovanim nosačima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO, nazvani Eupergit C250L-PFO; Celit-PFO i CelulozaM-PFO, testirani su u reaktoru za uklanjanje fenola, 4-hlorfenola i 4-bromfenola. U slučaju 2,5 mM supstrata sa Eupergit C250L-PFO, postignuto je oko 45 % razgradnje 4-bromfenola, dok su 4-hlorfenol i fenol razgrađeni 35, odnosno 20 %. Testirana je i sposobnost višestruke upotrebe Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola. Nakon osam ponovljenih ciklusa efikasnost Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola je pala na 55%.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase
T1  - Uklanjanje fenola i fenolnih derivata iz vode imobilizovanom polifenol-oksidazom iz krompira
VL  - 76
IS  - 4
SP  - 513
EP  - 522
DO  - 10.2298/JSC100619046L
ER  - 

@article{
author = "Lončar, Nikola and Božić, Nataša and Anđelković, Ivan and Milovanović, Aleksandra and Dojnov, Biljana and Vujčić, Miroslava and Roglić, Goran and Vujčić, Zoran",
year = "2011",
abstract = "Phenols containing halogens, which tend to deactivate the aromatic nuclei, constitute a significant category of highly toxic and difficult-to-degrade pollutants, which arise from a wide variety of industries. The main purpose of this study was to obtain an inexpensive immobilized enzyme for the removal of phenols. Partially purified potato polyphenol oxidase (PPO) was immobilized onto different commercial and laboratory produced carriers. Three of the obtained biocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO; Celite-PPO and CelluloseM-PPO, were tested in a batch reactor for the removal of phenol, 4-chlorophenol and 4-bromophenol. In the case of 2.5 mM substrates with Eupergit C250L-PPO, an around 45% removal of 4-bromophenol was achieved, while the removals 4-chlorophenol and phenol were 35 and 20%, respectively. The reusability of Eupergit C250L-PPO for the removal of 4-chlorophenol was tested. After eight repeated tests, the efficiency of 4-chlorophenol removal by Eupergit C250L-PPO immobilisate had decreased to 55%., Halogenovani fenoli imaju dezaktivirano aromatično jezgro i čine značajnu kategoriju veoma toksičnih i teško razgradivih zagađivača u raznim industrijskim granama. Glavni cilj ovog rada je bio dobijanje jeftinog imobilizovanog enzima za uklanjanje fenola. Delimično prečišćena polifenol-oksidaza (PFO) iz krompira je imobilizovana na različitim komercijalnim i laboratorijski sintetizovanim nosačima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO, nazvani Eupergit C250L-PFO; Celit-PFO i CelulozaM-PFO, testirani su u reaktoru za uklanjanje fenola, 4-hlorfenola i 4-bromfenola. U slučaju 2,5 mM supstrata sa Eupergit C250L-PFO, postignuto je oko 45 % razgradnje 4-bromfenola, dok su 4-hlorfenol i fenol razgrađeni 35, odnosno 20 %. Testirana je i sposobnost višestruke upotrebe Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola. Nakon osam ponovljenih ciklusa efikasnost Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola je pala na 55%.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase, Uklanjanje fenola i fenolnih derivata iz vode imobilizovanom polifenol-oksidazom iz krompira",
volume = "76",
number = "4",
pages = "513-522",
doi = "10.2298/JSC100619046L"
}

Lončar, N., Božić, N., Anđelković, I., Milovanović, A., Dojnov, B., Vujčić, M., Roglić, G.,& Vujčić, Z.. (2011). Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(4), 513-522.
https://doi.org/10.2298/JSC100619046L

Lončar N, Božić N, Anđelković I, Milovanović A, Dojnov B, Vujčić M, Roglić G, Vujčić Z. Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase. in Journal of the Serbian Chemical Society. 2011;76(4):513-522.
doi:10.2298/JSC100619046L .

Lončar, Nikola, Božić, Nataša, Anđelković, Ivan, Milovanović, Aleksandra, Dojnov, Biljana, Vujčić, Miroslava, Roglić, Goran, Vujčić, Zoran, "Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase" in Journal of the Serbian Chemical Society, 76, no. 4 (2011):513-522,
https://doi.org/10.2298/JSC100619046L . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/708
AB  - α-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI  LT  3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa.
AB  - Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI  LT  3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of Biological Sciences
T1  - Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet
T1  - Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi
VL  - 62
IS  - 3
SP  - 575
EP  - 584
DO  - 10.2298/ABS1003575D
ER  - 

@article{
author = "Dojnov, Biljana and Lončar, Nikola and Božić, Nataša and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2010",
abstract = "α-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI  LT  3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa., Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI  LT  3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of Biological Sciences",
title = "Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet, Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi",
volume = "62",
number = "3",
pages = "575-584",
doi = "10.2298/ABS1003575D"
}

Dojnov, B., Lončar, N., Božić, N., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2010). Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet. in Archives of Biological Sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 62(3), 575-584.
https://doi.org/10.2298/ABS1003575D

Dojnov B, Lončar N, Božić N, Nenadovic V, Ivanovic J, Vujčić Z. Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet. in Archives of Biological Sciences. 2010;62(3):575-584.
doi:10.2298/ABS1003575D .

Dojnov, Biljana, Lončar, Nikola, Božić, Nataša, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet" in Archives of Biological Sciences, 62, no. 3 (2010):575-584,
https://doi.org/10.2298/ABS1003575D . .

TY  - JOUR
AU  - Lončar, Nikola
AU  - Vujčić, Zoran
AU  - Božić, Nataša
AU  - Ivanovic, Jelisaveta
AU  - Nenadovic, Vera
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/706
AB  - Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K-I value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co2+ and Mn2+ stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer.
PB  - Wiley-Blackwell, Hoboken
T2  - Archives of Insect Biochemistry and Physiology
T1  - Purification and properties of trypsin-like enzyme from the midgut of morimus funereus (coleoptera, cerambycidae) larvae
VL  - 74
IS  - 4
SP  - 232
EP  - 246
DO  - 10.1002/arch.20371
ER  - 

@article{
author = "Lončar, Nikola and Vujčić, Zoran and Božić, Nataša and Ivanovic, Jelisaveta and Nenadovic, Vera",
year = "2010",
abstract = "Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K-I value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co2+ and Mn2+ stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Archives of Insect Biochemistry and Physiology",
title = "Purification and properties of trypsin-like enzyme from the midgut of morimus funereus (coleoptera, cerambycidae) larvae",
volume = "74",
number = "4",
pages = "232-246",
doi = "10.1002/arch.20371"
}

Lončar, N., Vujčić, Z., Božić, N., Ivanovic, J.,& Nenadovic, V.. (2010). Purification and properties of trypsin-like enzyme from the midgut of morimus funereus (coleoptera, cerambycidae) larvae. in Archives of Insect Biochemistry and Physiology
Wiley-Blackwell, Hoboken., 74(4), 232-246.
https://doi.org/10.1002/arch.20371

Lončar N, Vujčić Z, Božić N, Ivanovic J, Nenadovic V. Purification and properties of trypsin-like enzyme from the midgut of morimus funereus (coleoptera, cerambycidae) larvae. in Archives of Insect Biochemistry and Physiology. 2010;74(4):232-246.
doi:10.1002/arch.20371 .

Lončar, Nikola, Vujčić, Zoran, Božić, Nataša, Ivanovic, Jelisaveta, Nenadovic, Vera, "Purification and properties of trypsin-like enzyme from the midgut of morimus funereus (coleoptera, cerambycidae) larvae" in Archives of Insect Biochemistry and Physiology, 74, no. 4 (2010):232-246,
https://doi.org/10.1002/arch.20371 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Milovanović, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Anđelković, Uroš
AU  - Lončar, Nikola
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/678
AB  - Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.
PB  - American Chemical Society (ACS)
T2  - Journal of Agricultural and Food Chemistry
T1  - Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar
VL  - 58
IS  - 22
SP  - 11896
EP  - 11900
DO  - 10.1021/jf101836r
ER  - 

@article{
author = "Vujčić, Zoran and Milovanović, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava and Anđelković, Uroš and Lončar, Nikola",
year = "2010",
abstract = "Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.",
publisher = "American Chemical Society (ACS)",
journal = "Journal of Agricultural and Food Chemistry",
title = "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar",
volume = "58",
number = "22",
pages = "11896-11900",
doi = "10.1021/jf101836r"
}

Vujčić, Z., Milovanović, A., Božić, N., Dojnov, B., Vujčić, M., Anđelković, U.,& Lončar, N.. (2010). Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry
American Chemical Society (ACS)., 58(22), 11896-11900.
https://doi.org/10.1021/jf101836r

Vujčić Z, Milovanović A, Božić N, Dojnov B, Vujčić M, Anđelković U, Lončar N. Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry. 2010;58(22):11896-11900.
doi:10.1021/jf101836r .

Vujčić, Zoran, Milovanović, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, Anđelković, Uroš, Lončar, Nikola, "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar" in Journal of Agricultural and Food Chemistry, 58, no. 22 (2010):11896-11900,
https://doi.org/10.1021/jf101836r . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Lončar, Nikola
AU  - Dojnov, Biljana
AU  - Milovanović, Aleksandra
AU  - Vujčić, Miroslava
AU  - Božić, Nataša
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/698
AB  - Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber
VL  - 121
IS  - 2
SP  - 418
EP  - 423
DO  - 10.1016/j.foodchem.2009.12.058
ER  - 

@article{
author = "Vujčić, Zoran and Lončar, Nikola and Dojnov, Biljana and Milovanović, Aleksandra and Vujčić, Miroslava and Božić, Nataša",
year = "2010",
abstract = "Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber",
volume = "121",
number = "2",
pages = "418-423",
doi = "10.1016/j.foodchem.2009.12.058"
}

Vujčić, Z., Lončar, N., Dojnov, B., Milovanović, A., Vujčić, M.,& Božić, N.. (2010). Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry
Elsevier Sci Ltd, Oxford., 121(2), 418-423.
https://doi.org/10.1016/j.foodchem.2009.12.058

Vujčić Z, Lončar N, Dojnov B, Milovanović A, Vujčić M, Božić N. Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry. 2010;121(2):418-423.
doi:10.1016/j.foodchem.2009.12.058 .

Vujčić, Zoran, Lončar, Nikola, Dojnov, Biljana, Milovanović, Aleksandra, Vujčić, Miroslava, Božić, Nataša, "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber" in Food Chemistry, 121, no. 2 (2010):418-423,
https://doi.org/10.1016/j.foodchem.2009.12.058 . .

TY  - JOUR
AU  - Lončar, Nikola
AU  - Božić, Nataša
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/562
AB  - The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine.
AB  - pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.
PB  - University of Belgrade, University of Novi Sad
T2  - Archives of Biological Sciences
T1  - Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae
T1  - Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
VL  - 61
IS  - 4
SP  - 713
EP  - 718
DO  - 10.2298/ABS0904713L
ER  - 

@article{
author = "Lončar, Nikola and Božić, Nataša and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran",
year = "2009",
abstract = "The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine., pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.",
publisher = "University of Belgrade, University of Novi Sad",
journal = "Archives of Biological Sciences",
title = "Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae, Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)",
volume = "61",
number = "4",
pages = "713-718",
doi = "10.2298/ABS0904713L"
}

Lončar, N., Božić, N., Nenadović, V., Ivanović, J.,& Vujčić, Z.. (2009). Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae. in Archives of Biological Sciences
University of Belgrade, University of Novi Sad., 61(4), 713-718.
https://doi.org/10.2298/ABS0904713L

Lončar N, Božić N, Nenadović V, Ivanović J, Vujčić Z. Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae. in Archives of Biological Sciences. 2009;61(4):713-718.
doi:10.2298/ABS0904713L .

Lončar, Nikola, Božić, Nataša, Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran, "Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae" in Archives of Biological Sciences, 61, no. 4 (2009):713-718,
https://doi.org/10.2298/ABS0904713L . .