Božić, Nataša

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  • Božić, Nataša (47)

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

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

(2020)

TY  - JOUR
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Lončar, Nikola L.
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh P.
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3356
AB  - Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7–24 h with good yields (70–99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 °C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.
T2  - Enzyme and Microbial Technology
T1  - Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
VL  - 132
DO  - 10.1016/j.enzmictec.2019.109411
ER  - 
@article{
author = "Simić, Stefan and Jeremić, Sanja and Đokić, Lidija and Božić, Nataša and Vujčić, Zoran and Lončar, Nikola L. and Senthamaraikannan, Ramsankar and Babu, Ramesh P. and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7–24 h with good yields (70–99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 °C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.",
journal = "Enzyme and Microbial Technology",
title = "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines",
volume = "132",
doi = "10.1016/j.enzmictec.2019.109411"
}
Simić, S., Jeremić, S., Đokić, L., Božić, N., Vujčić, Z., Lončar, N. L., Senthamaraikannan, R., Babu, R. P., Opsenica, I.,& Nikodinović-Runić, J.. (2020). Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology, 132.
https://doi.org/10.1016/j.enzmictec.2019.109411
Simić S, Jeremić S, Đokić L, Božić N, Vujčić Z, Lončar NL, Senthamaraikannan R, Babu RP, Opsenica I, Nikodinović-Runić J. Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology. 2020;132.
doi:10.1016/j.enzmictec.2019.109411 .
Simić, Stefan, Jeremić, Sanja, Đokić, Lidija, Božić, Nataša, Vujčić, Zoran, Lončar, Nikola L., Senthamaraikannan, Ramsankar, Babu, Ramesh P., Opsenica, Igor, Nikodinović-Runić, Jasmina, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" in Enzyme and Microbial Technology, 132 (2020),
https://doi.org/10.1016/j.enzmictec.2019.109411 . .
6
3
5

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

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

(2020)

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

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

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

(MDPI, 2019)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Drašković, Natalija
AU  - Božić, Nataša
AU  - Romero, Elvira
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Vujčić, Zoran
AU  - Fraaije, Marco W.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3709
AB  - The consumption of dyes is increasing worldwide in line with the increase of population and demand for clothes and other colored products. However, the efficiency of dyeing processes is still poor and results in large amounts of colored effluents. It is desired to develop a portfolio of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30◦ C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.
PB  - MDPI
T2  - Catalysts
T1  - Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1
VL  - 9
IS  - 5
DO  - 10.3390/catal9050463
ER  - 
@article{
author = "Lončar, Nikola L. and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
abstract = "The consumption of dyes is increasing worldwide in line with the increase of population and demand for clothes and other colored products. However, the efficiency of dyeing processes is still poor and results in large amounts of colored effluents. It is desired to develop a portfolio of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30◦ C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.",
publisher = "MDPI",
journal = "Catalysts",
title = "Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1",
volume = "9",
number = "5",
doi = "10.3390/catal9050463"
}
Lončar, N. L., Drašković, N., Božić, N., Romero, E., Simić, S., Opsenica, I., Vujčić, Z.,& Fraaije, M. W.. (2019). Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1. in Catalysts
MDPI., 9(5).
https://doi.org/10.3390/catal9050463
Lončar NL, Drašković N, Božić N, Romero E, Simić S, Opsenica I, Vujčić Z, Fraaije MW. Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1. in Catalysts. 2019;9(5).
doi:10.3390/catal9050463 .
Lončar, Nikola L., Drašković, Natalija, Božić, Nataša, Romero, Elvira, Simić, Stefan, Opsenica, Igor, Vujčić, Zoran, Fraaije, Marco W., "Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1" in Catalysts, 9, no. 5 (2019),
https://doi.org/10.3390/catal9050463 . .
1
5
4
5

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

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

(MDPI, 2019)

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

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

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

(Springer, New York, 2016)

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

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

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

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3517
AB  - Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
VL  - 134
SP  - 390
EP  - 395
DO  - 10.1016/j.molcatb.2016.06.005
UR  - Kon_3191
ER  - 
@article{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
abstract = "Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a",
volume = "134",
pages = "390-395",
doi = "10.1016/j.molcatb.2016.06.005",
url = "Kon_3191"
}
Lončar, N. L., Božić, N.,& Vujčić, Z.. (2016). Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam., 134, 390-395.
https://doi.org/10.1016/j.molcatb.2016.06.005
Kon_3191
Lončar NL, Božić N, Vujčić Z. Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005
Kon_3191 .
Lončar, Nikola L., Božić, Nataša, Vujčić, Zoran, "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a" in Journal of Molecular Catalysis. B: Enzymatic, 134 (2016):390-395,
https://doi.org/10.1016/j.molcatb.2016.06.005 .,
Kon_3191 .
13
12
13

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

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

(Elsevier Science Bv, Amsterdam, 2016)

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

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

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

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2375
AB  - Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
VL  - 134
SP  - 390
EP  - 395
DO  - 10.1016/j.molcatb.2016.06.005
UR  - Kon_3191
ER  - 
@article{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
abstract = "Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a",
volume = "134",
pages = "390-395",
doi = "10.1016/j.molcatb.2016.06.005",
url = "Kon_3191"
}
Lončar, N. L., Božić, N.,& Vujčić, Z.. (2016). Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam., 134, 390-395.
https://doi.org/10.1016/j.molcatb.2016.06.005
Kon_3191
Lončar NL, Božić N, Vujčić Z. Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005
Kon_3191 .
Lončar, Nikola L., Božić, Nataša, Vujčić, Zoran, "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a" in Journal of Molecular Catalysis. B: Enzymatic, 134 (2016):390-395,
https://doi.org/10.1016/j.molcatb.2016.06.005 .,
Kon_3191 .
13
12
13

Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase

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

(Springer, New York, 2016)

TY  - JOUR
AU  - Šokarda-Slavić, Marinela
AU  - Pešić, Milja
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2061
AB  - alpha-Amylase from Bacillus licheniformis ATCC 9945a (BliAmy) was proven to be very efficient in hydrolysis of granular starch below the temperature of gelatinization. By applying two-stage feeding strategy to achieve high-cell-density cultivation of Escherichia coli and extracellular production of BliAmy, total of 250.5 U/mL (i.e. 0.7 g/L) of enzyme was obtained. Thermostability of amylase was exploited to simplify purification. The hydrolysis of concentrated raw starch was optimized using response surface methodology. Regardless of raw starch concentration tested (20, 25, 30 %), BliAmy was very effective, achieving the final hydrolysis degree of 91 % for the hydrolysis of 30 % starch suspension after 24 h. The major A-type crystalline structure and amorphous domains of the starch granule were degraded at the same rates, while amylose-lipid complexes were not degraded. BliAmy presents interesting performances on highly concentrated solid starch and could be of value for starch-consuming industries while response surface methodology (RSM) could be efficiently applied for the optimization of the hydrolysis.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase
VL  - 100
IS  - 6
SP  - 2709
EP  - 2719
DO  - 10.1007/s00253-015-7101-4
UR  - Kon_3017
ER  - 
@article{
author = "Šokarda-Slavić, Marinela and Pešić, Milja and Vujčić, Zoran and Božić, Nataša",
year = "2016",
abstract = "alpha-Amylase from Bacillus licheniformis ATCC 9945a (BliAmy) was proven to be very efficient in hydrolysis of granular starch below the temperature of gelatinization. By applying two-stage feeding strategy to achieve high-cell-density cultivation of Escherichia coli and extracellular production of BliAmy, total of 250.5 U/mL (i.e. 0.7 g/L) of enzyme was obtained. Thermostability of amylase was exploited to simplify purification. The hydrolysis of concentrated raw starch was optimized using response surface methodology. Regardless of raw starch concentration tested (20, 25, 30 %), BliAmy was very effective, achieving the final hydrolysis degree of 91 % for the hydrolysis of 30 % starch suspension after 24 h. The major A-type crystalline structure and amorphous domains of the starch granule were degraded at the same rates, while amylose-lipid complexes were not degraded. BliAmy presents interesting performances on highly concentrated solid starch and could be of value for starch-consuming industries while response surface methodology (RSM) could be efficiently applied for the optimization of the hydrolysis.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase",
volume = "100",
number = "6",
pages = "2709-2719",
doi = "10.1007/s00253-015-7101-4",
url = "Kon_3017"
}
Šokarda-Slavić, M., Pešić, M., Vujčić, Z.,& Božić, N.. (2016). Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase. in Applied Microbiology and Biotechnology
Springer, New York., 100(6), 2709-2719.
https://doi.org/10.1007/s00253-015-7101-4
Kon_3017
Šokarda-Slavić M, Pešić M, Vujčić Z, Božić N. Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase. in Applied Microbiology and Biotechnology. 2016;100(6):2709-2719.
doi:10.1007/s00253-015-7101-4
Kon_3017 .
Šokarda-Slavić, Marinela, Pešić, Milja, Vujčić, Zoran, Božić, Nataša, "Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase" in Applied Microbiology and Biotechnology, 100, no. 6 (2016):2709-2719,
https://doi.org/10.1007/s00253-015-7101-4 .,
Kon_3017 .
13
9
10

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

Lončar, Nikola L.; Šokarda-Slavić, Marinela; Vujčić, Zoran; Božić, Nataša

(Nature Publishing Group, London, 2015)

TY  - DATA
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3384
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772
ER  - 
@misc{
author = "Lončar, Nikola L. and Šokarda-Slavić, Marinela and Vujčić, Zoran and Božić, Nataša",
year = "2015",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772"
}
Lončar, N. L., Šokarda-Slavić, M., Vujčić, Z.,& Božić, N.. (2015). Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772. in Scientific Reports
Nature Publishing Group, London..
Lončar NL, Šokarda-Slavić M, Vujčić Z, Božić N. Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772. in Scientific Reports. 2015;..
Lončar, Nikola L., Šokarda-Slavić, Marinela, Vujčić, Zoran, Božić, Nataša, "Supplementary data for article: Lončar, N.; Slavić, M. Š.; Vujčić, Z.; Božić, N. Mixed-Mode Resins: Taking Shortcut in Downstream Processing of Raw-Starch Digesting α-Amylases. Scientific Reports 2015, 5. https://doi.org/10.1038/srep15772" in Scientific Reports (2015).

Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization

Vujčić, Zoran; Janović, Barbara; Lončar, Nikola L.; Margetić, Aleksandra; Božić, Nataša; Dojnov, Biljana; Vujčić, Miroslava

(Elsevier Sci Ltd, Oxford, 2015)

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Janović, Barbara
AU  - Lončar, Nikola L.
AU  - Margetić, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1644
AB  - Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization
VL  - 97
SP  - 124
EP  - 127
DO  - 10.1016/j.ibiod.2014.10.007
UR  - Kon_2790
ER  - 
@article{
author = "Vujčić, Zoran and Janović, Barbara and Lončar, Nikola L. and Margetić, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava",
year = "2015",
abstract = "Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization",
volume = "97",
pages = "124-127",
doi = "10.1016/j.ibiod.2014.10.007",
url = "Kon_2790"
}
Vujčić, Z., Janović, B., Lončar, N. L., Margetić, A., Božić, N., Dojnov, B.,& Vujčić, M.. (2015). Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 97, 124-127.
https://doi.org/10.1016/j.ibiod.2014.10.007
Kon_2790
Vujčić Z, Janović B, Lončar NL, Margetić A, Božić N, Dojnov B, Vujčić M. Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation. 2015;97:124-127.
doi:10.1016/j.ibiod.2014.10.007
Kon_2790 .
Vujčić, Zoran, Janović, Barbara, Lončar, Nikola L., Margetić, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization" in International Biodeterioration and Biodegradation, 97 (2015):124-127,
https://doi.org/10.1016/j.ibiod.2014.10.007 .,
Kon_2790 .
3
7
8
9

Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases

Lončar, Nikola L.; Šokarda-Slavić, Marinela; Vujčić, Zoran; Božić, Nataša

(Nature Publishing Group, London, 2015)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Šokarda-Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1985
AB  - Bacillus licheniformis 9945a alpha-amylase is known as a potent enzyme for raw starch hydrolysis. In this paper, a mixed mode Nuvia cPrime (TM) resin is examined with the aim to improve the downstream processing of raw starch digesting amylases and exploit the hydrophobic patches on their surface. This resin combines hydrophobic interactions with cation exchange groups and as such the presence of salt facilitates hydrophobic interactions while the ion-exchange groups enable proper selectivity. alpha-Amylase was produced using an optimized fed-batch approach in a defined media and significant overexpression of 1.2 g L-1 was achieved. This single step procedure enables simultaneous concentration, pigment removal as well as purification of amylase with yields of 96% directly from the fermentation broth.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases
VL  - 5
DO  - 10.1038/srep15772
UR  - Kon_2940
ER  - 
@article{
author = "Lončar, Nikola L. and Šokarda-Slavić, Marinela and Vujčić, Zoran and Božić, Nataša",
year = "2015",
abstract = "Bacillus licheniformis 9945a alpha-amylase is known as a potent enzyme for raw starch hydrolysis. In this paper, a mixed mode Nuvia cPrime (TM) resin is examined with the aim to improve the downstream processing of raw starch digesting amylases and exploit the hydrophobic patches on their surface. This resin combines hydrophobic interactions with cation exchange groups and as such the presence of salt facilitates hydrophobic interactions while the ion-exchange groups enable proper selectivity. alpha-Amylase was produced using an optimized fed-batch approach in a defined media and significant overexpression of 1.2 g L-1 was achieved. This single step procedure enables simultaneous concentration, pigment removal as well as purification of amylase with yields of 96% directly from the fermentation broth.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases",
volume = "5",
doi = "10.1038/srep15772",
url = "Kon_2940"
}
Lončar, N. L., Šokarda-Slavić, M., Vujčić, Z.,& Božić, N.. (2015). Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases. in Scientific Reports
Nature Publishing Group, London., 5.
https://doi.org/10.1038/srep15772
Kon_2940
Lončar NL, Šokarda-Slavić M, Vujčić Z, Božić N. Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases. in Scientific Reports. 2015;5.
doi:10.1038/srep15772
Kon_2940 .
Lončar, Nikola L., Šokarda-Slavić, Marinela, Vujčić, Zoran, Božić, Nataša, "Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylases" in Scientific Reports, 5 (2015),
https://doi.org/10.1038/srep15772 .,
Kon_2940 .
1
5
3
4

A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia

Gligorijević, Nikola; Stevanović, Nikola R.; Lončar, Nikola L.; Baošić, Rada; Vujčić, Zoran; Božić, Nataša

(Serbian Chemical Soc, Belgrade, 2014)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stevanović, Nikola R.
AU  - Lončar, Nikola L.
AU  - Baošić, Rada
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1771
AB  - Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia
VL  - 79
IS  - 4
SP  - 411
EP  - 420
DO  - 10.2298/JSC130909155G
UR  - Kon_2654
ER  - 
@article{
author = "Gligorijević, Nikola and Stevanović, Nikola R. and Lončar, Nikola L. and Baošić, Rada and Vujčić, Zoran and Božić, Nataša",
year = "2014",
abstract = "Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia",
volume = "79",
number = "4",
pages = "411-420",
doi = "10.2298/JSC130909155G",
url = "Kon_2654"
}
Gligorijević, N., Stevanović, N. R., Lončar, N. L., Baošić, R., Vujčić, Z.,& Božić, N.. (2014). A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 79(4), 411-420.
https://doi.org/10.2298/JSC130909155G
Kon_2654
Gligorijević N, Stevanović NR, Lončar NL, Baošić R, Vujčić Z, Božić N. A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society. 2014;79(4):411-420.
doi:10.2298/JSC130909155G
Kon_2654 .
Gligorijević, Nikola, Stevanović, Nikola R., Lončar, Nikola L., Baošić, Rada, Vujčić, Zoran, Božić, Nataša, "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia" in Journal of the Serbian Chemical Society, 79, no. 4 (2014):411-420,
https://doi.org/10.2298/JSC130909155G .,
Kon_2654 .
2
2
2

Chemical modification of chloroperoxidase for enhanced stability and activity

Pešić, Milja; Božić, Nataša; Lopez, Carmen; Lončar, Nikola L.; Alvaro, Gregorio; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3743
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
UR  - Kon_2727
ER  - 
@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025",
url = "Kon_2727"
}
Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025
Kon_2727
Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025
Kon_2727 .
Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 .,
Kon_2727 .
4
5
5

Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases

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

(Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd, 2014)

TY  - JOUR
AU  - Šokarda-Slavić, Marinela
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1850
AB  - Natural amylase producers, wild type strains of Bacillus sp., were isolated from different regions of Serbia. Strains with the highest amylase activity based on the starch-agar plate test were grown on solid-state fermentation (SSF) on triticale. The influence of the substrate and different cultivation temperature (28 and 37 degrees C) on the production of amylase was examined. The tested strains produced alpha-amylases when grown on triticale grains both at 28 and at 37 degrees C, but the activity of amylases and the number and intensity of the produced isoforms were different. Significant hydrolysis of raw cornstarch was obtained with the Bacillus sp. strains 2B, 5B, 18 and 24B. The produced alpha-amylases hydrolyzed raw cornstarch at a temperature below the temperature of gelatinization, but the ability for hydrolysis was not directly related to the total enzyme activity, suggesting that only certain isoforms are involved in the hydrolysis.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases
VL  - 66
IS  - 2
SP  - 483
EP  - 490
DO  - 10.2298/ABS1402483S
UR  - Kon_2733
ER  - 
@article{
author = "Šokarda-Slavić, Marinela and Božić, Nataša and Vujčić, Zoran",
year = "2014",
abstract = "Natural amylase producers, wild type strains of Bacillus sp., were isolated from different regions of Serbia. Strains with the highest amylase activity based on the starch-agar plate test were grown on solid-state fermentation (SSF) on triticale. The influence of the substrate and different cultivation temperature (28 and 37 degrees C) on the production of amylase was examined. The tested strains produced alpha-amylases when grown on triticale grains both at 28 and at 37 degrees C, but the activity of amylases and the number and intensity of the produced isoforms were different. Significant hydrolysis of raw cornstarch was obtained with the Bacillus sp. strains 2B, 5B, 18 and 24B. The produced alpha-amylases hydrolyzed raw cornstarch at a temperature below the temperature of gelatinization, but the ability for hydrolysis was not directly related to the total enzyme activity, suggesting that only certain isoforms are involved in the hydrolysis.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases",
volume = "66",
number = "2",
pages = "483-490",
doi = "10.2298/ABS1402483S",
url = "Kon_2733"
}
Šokarda-Slavić, M., Božić, N.,& Vujčić, Z.. (2014). Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 66(2), 483-490.
https://doi.org/10.2298/ABS1402483S
Kon_2733
Šokarda-Slavić M, Božić N, Vujčić Z. Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases. in Archives of biological sciences. 2014;66(2):483-490.
doi:10.2298/ABS1402483S
Kon_2733 .
Šokarda-Slavić, Marinela, Božić, Nataša, Vujčić, Zoran, "Growth Temperature of Different Local Isolates of Bacillus Sp in the Solid State Affects Production of Raw Starch Digesting Amylases" in Archives of biological sciences, 66, no. 2 (2014):483-490,
https://doi.org/10.2298/ABS1402483S .,
Kon_2733 .

Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia

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

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Gligorijević, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1791
AB  - Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia
VL  - 91
SP  - 18
EP  - 23
DO  - 10.1016/j.ibiod.2014.03.008
UR  - Kon_2674
ER  - 
@article{
author = "Lončar, Nikola L. and Gligorijević, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2014",
abstract = "Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia",
volume = "91",
pages = "18-23",
doi = "10.1016/j.ibiod.2014.03.008",
url = "Kon_2674"
}
Lončar, N. L., Gligorijević, N., Božić, N.,& Vujčić, Z.. (2014). Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 91, 18-23.
https://doi.org/10.1016/j.ibiod.2014.03.008
Kon_2674
Lončar NL, Gligorijević N, Božić N, Vujčić Z. Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation. 2014;91:18-23.
doi:10.1016/j.ibiod.2014.03.008
Kon_2674 .
Lončar, Nikola L., Gligorijević, Nikola, Božić, Nataša, Vujčić, Zoran, "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia" in International Biodeterioration and Biodegradation, 91 (2014):18-23,
https://doi.org/10.1016/j.ibiod.2014.03.008 .,
Kon_2674 .
16
18
21

Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization

Božić, Nataša; Šokarda-Slavić, Marinela; Gavrilović, Anja; Vujčić, Zoran

(Springer, New York, 2014)

TY  - JOUR
AU  - Božić, Nataša
AU  - Šokarda-Slavić, Marinela
AU  - Gavrilović, Anja
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1798
AB  - alpha-Amylase production by solid-state fermentation of different Bacillus sp. was studied previously on different fermentation media. However, no study has been reported on the influence of selected media on expression of desired amylase isoforms such as raw-starch-digesting amylase (RSDA). In this paper, the influence of different inexpensive and available agro-resources as solid media (corn, wheat and triticale) on alpha-amylase isoform induction from three wild-type Bacillus sp., selected among one hundred strains tested, namely 9B, 12B and 24A was investigated. For all three strains, tested amylases were detected in the multiple forms; however, number and intensity of each form differed depending on the solid media used for growth. To determine which isoform from Bacillus sp. 12B was RSDA, the suspected isoform was purified. The optimum pH for the purified alpha-amylase isoform was 6.0-8.0, while the optimum temperature was 60-90 A degrees C. Isoform was considerably thermostable and Ca2+-independent, and actually the only alpha-amylase active towards raw starch. Purification and characterization of RSDA showed that not all of the solid media tested induced RSDA. From an economic point of view, it might be significant to obtain pure isoenzyme for potential use in the raw-starch hydrolysis, since it was 5 times more efficient in raw corn starch hydrolysis than the crude amylase preparation.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization
VL  - 37
IS  - 7
SP  - 1353
EP  - 1360
DO  - 10.1007/s00449-013-1105-1
UR  - Kon_2681
ER  - 
@article{
author = "Božić, Nataša and Šokarda-Slavić, Marinela and Gavrilović, Anja and Vujčić, Zoran",
year = "2014",
abstract = "alpha-Amylase production by solid-state fermentation of different Bacillus sp. was studied previously on different fermentation media. However, no study has been reported on the influence of selected media on expression of desired amylase isoforms such as raw-starch-digesting amylase (RSDA). In this paper, the influence of different inexpensive and available agro-resources as solid media (corn, wheat and triticale) on alpha-amylase isoform induction from three wild-type Bacillus sp., selected among one hundred strains tested, namely 9B, 12B and 24A was investigated. For all three strains, tested amylases were detected in the multiple forms; however, number and intensity of each form differed depending on the solid media used for growth. To determine which isoform from Bacillus sp. 12B was RSDA, the suspected isoform was purified. The optimum pH for the purified alpha-amylase isoform was 6.0-8.0, while the optimum temperature was 60-90 A degrees C. Isoform was considerably thermostable and Ca2+-independent, and actually the only alpha-amylase active towards raw starch. Purification and characterization of RSDA showed that not all of the solid media tested induced RSDA. From an economic point of view, it might be significant to obtain pure isoenzyme for potential use in the raw-starch hydrolysis, since it was 5 times more efficient in raw corn starch hydrolysis than the crude amylase preparation.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization",
volume = "37",
number = "7",
pages = "1353-1360",
doi = "10.1007/s00449-013-1105-1",
url = "Kon_2681"
}
Božić, N., Šokarda-Slavić, M., Gavrilović, A.,& Vujčić, Z.. (2014). Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization. in Bioprocess and Biosystems Engineering
Springer, New York., 37(7), 1353-1360.
https://doi.org/10.1007/s00449-013-1105-1
Kon_2681
Božić N, Šokarda-Slavić M, Gavrilović A, Vujčić Z. Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization. in Bioprocess and Biosystems Engineering. 2014;37(7):1353-1360.
doi:10.1007/s00449-013-1105-1
Kon_2681 .
Božić, Nataša, Šokarda-Slavić, Marinela, Gavrilović, Anja, Vujčić, Zoran, "Production of raw-starch-digesting alpha-amylase isoform from Bacillus sp under solid-state fermentation and biochemical characterization" in Bioprocess and Biosystems Engineering, 37, no. 7 (2014):1353-1360,
https://doi.org/10.1007/s00449-013-1105-1 .,
Kon_2681 .
7
7
7

Chemical modification of chloroperoxidase for enhanced stability and activity

Pešić, Milja; Božić, Nataša; Lopez, Carmen; Lončar, Nikola L.; Alvaro, Gregorio; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1844
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
UR  - Kon_2727
ER  - 
@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025",
url = "Kon_2727"
}
Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025
Kon_2727
Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025
Kon_2727 .
Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 .,
Kon_2727 .
4
5
5

Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse

Popovic, Vesna; Atanasijevic, Tatjana; Nikolic, Slobodan; Božić, Nataša; Vujčić, Zoran; Micic-Labudovic, Jelena

(Srpsko Lekarsko Drustvo, Beograd, 2013)

TY  - JOUR
AU  - Popovic, Vesna
AU  - Atanasijevic, Tatjana
AU  - Nikolic, Slobodan
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Micic-Labudovic, Jelena
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1353
AB  - Introduction Carbohydrate-deficient transferrin (CDT) has been suggested as one of alcohol abuse indicators having produced good results in forensic medicine for years. Objective The aim of the study was to identify correlation between present methodology of alcohol abuse diagnosis at autopsy (macroscopic and microscopic findings) and CDT examination using the method of isoelectrofocusing (IEF) in polyacrylamide gel electrophoresis (PAGE). We also analyzed if the time interval between the moment of death and blood sample collection influences CDT findings. Methods The method used for CDT analysis was IEF-PAGE. Sera of 49 males and 11 females aged 14-87 years, average age 46.85 +/- 18.53, were used in this study. Control group consisted of five patients who died after medical treatment that lasted longer than 15 days, and five patients who started Disulfiram therapy in controlled hospital environment. Results The results obtained in CDT examination in dead bodies' sera showed sensitivity 59% and specificity 71%. A high incidence of falsely positive CDT result was noticed in liver failure and cirrhosis of non-alcoholic origin. CDT analysis is also possible to be done in samples collected postmortem up to 76 hours. Conclusion In forensic medicine, the method of CDT determination is reliable for the diagnosis of alcohol abuse.
AB  - Uvod. Poslednjih godina transferin s nedostatkom ugljenih hidrata (engl. carbohydrate-deficient transferrin - CDT) jedan je od markera zloupotrebe alkohola koji je pokazao najbolje rezultate u sudskoj medicini. Cilj rada. Cilj studije je bio da se odredi korelacija između aktuelne metodologije dijagnoze zloupotrebe alkohola na postmortalnom materijalu (makroskopski i mikroskopski nalaz) i određivanja CDT korišćenjem metode isoelektrofokusiranja (engl. isoelectric focusing - IEF) u poliakrilamidnom gelu (engl. polyacrylamide gel electrophoresis - PAGE). Utvrđivano je da li interval između vremena smrti i uzimanja uzoraka za CDT analizu utiče na nalaz CDT. Metode rada. Za analizu CDT korišćena je metoda IEF-PAGE. Za studiju su analizirani serumi 49 muškaraca i 11 žena prosečne starosti od 46,85±18,53 godina (raspon 14-87 godina). Kontrolnu grupu činilo je pet pacijenata koji su umrli nakon bolničkog lečenja koje je trajalo duže od 15 dana i pet pacijenata kod kojih je u kontrolisanim bolničkim uslovima počelo lečenje disulfiramom. Rezultati. Dobijeni rezultati pokazuju da ova metoda analize CDT na postmortalnom materijalu ima senzitivnost od 59% i specifičnost od 71%. Visoka učestalost lažno pozitivnih rezultata utvrđena je kod oboljenja jetre i ci- roze nealkoholnog porekla. Analizu CDT je moguće raditi i iz uzoraka uzetih do 76 sati nakon smrti. Zaključak. U sudskomedicinskoj praksi ova metoda analize CDT može se koristiti za dijagnostikovanje hronične zloupotrebe alkohola.
PB  - Srpsko Lekarsko Drustvo, Beograd
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse
T1  - Forenzički aspekti postmortalne analize transferina s nedostatkom ugljenih hidrata kao markera zloupotrebe alkohola
VL  - 141
IS  - 3-4
SP  - 203
EP  - 206
DO  - 10.2298/SARH1304203P
UR  - Kon_2473
ER  - 
@article{
author = "Popovic, Vesna and Atanasijevic, Tatjana and Nikolic, Slobodan and Božić, Nataša and Vujčić, Zoran and Micic-Labudovic, Jelena",
year = "2013",
abstract = "Introduction Carbohydrate-deficient transferrin (CDT) has been suggested as one of alcohol abuse indicators having produced good results in forensic medicine for years. Objective The aim of the study was to identify correlation between present methodology of alcohol abuse diagnosis at autopsy (macroscopic and microscopic findings) and CDT examination using the method of isoelectrofocusing (IEF) in polyacrylamide gel electrophoresis (PAGE). We also analyzed if the time interval between the moment of death and blood sample collection influences CDT findings. Methods The method used for CDT analysis was IEF-PAGE. Sera of 49 males and 11 females aged 14-87 years, average age 46.85 +/- 18.53, were used in this study. Control group consisted of five patients who died after medical treatment that lasted longer than 15 days, and five patients who started Disulfiram therapy in controlled hospital environment. Results The results obtained in CDT examination in dead bodies' sera showed sensitivity 59% and specificity 71%. A high incidence of falsely positive CDT result was noticed in liver failure and cirrhosis of non-alcoholic origin. CDT analysis is also possible to be done in samples collected postmortem up to 76 hours. Conclusion In forensic medicine, the method of CDT determination is reliable for the diagnosis of alcohol abuse., Uvod. Poslednjih godina transferin s nedostatkom ugljenih hidrata (engl. carbohydrate-deficient transferrin - CDT) jedan je od markera zloupotrebe alkohola koji je pokazao najbolje rezultate u sudskoj medicini. Cilj rada. Cilj studije je bio da se odredi korelacija između aktuelne metodologije dijagnoze zloupotrebe alkohola na postmortalnom materijalu (makroskopski i mikroskopski nalaz) i određivanja CDT korišćenjem metode isoelektrofokusiranja (engl. isoelectric focusing - IEF) u poliakrilamidnom gelu (engl. polyacrylamide gel electrophoresis - PAGE). Utvrđivano je da li interval između vremena smrti i uzimanja uzoraka za CDT analizu utiče na nalaz CDT. Metode rada. Za analizu CDT korišćena je metoda IEF-PAGE. Za studiju su analizirani serumi 49 muškaraca i 11 žena prosečne starosti od 46,85±18,53 godina (raspon 14-87 godina). Kontrolnu grupu činilo je pet pacijenata koji su umrli nakon bolničkog lečenja koje je trajalo duže od 15 dana i pet pacijenata kod kojih je u kontrolisanim bolničkim uslovima počelo lečenje disulfiramom. Rezultati. Dobijeni rezultati pokazuju da ova metoda analize CDT na postmortalnom materijalu ima senzitivnost od 59% i specifičnost od 71%. Visoka učestalost lažno pozitivnih rezultata utvrđena je kod oboljenja jetre i ci- roze nealkoholnog porekla. Analizu CDT je moguće raditi i iz uzoraka uzetih do 76 sati nakon smrti. Zaključak. U sudskomedicinskoj praksi ova metoda analize CDT može se koristiti za dijagnostikovanje hronične zloupotrebe alkohola.",
publisher = "Srpsko Lekarsko Drustvo, Beograd",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse, Forenzički aspekti postmortalne analize transferina s nedostatkom ugljenih hidrata kao markera zloupotrebe alkohola",
volume = "141",
number = "3-4",
pages = "203-206",
doi = "10.2298/SARH1304203P",
url = "Kon_2473"
}
Popovic, V., Atanasijevic, T., Nikolic, S., Božić, N., Vujčić, Z.,& Micic-Labudovic, J.. (2013). Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse. in Srpski arhiv za celokupno lekarstvo
Srpsko Lekarsko Drustvo, Beograd., 141(3-4), 203-206.
https://doi.org/10.2298/SARH1304203P
Kon_2473
Popovic V, Atanasijevic T, Nikolic S, Božić N, Vujčić Z, Micic-Labudovic J. Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse. in Srpski arhiv za celokupno lekarstvo. 2013;141(3-4):203-206.
doi:10.2298/SARH1304203P
Kon_2473 .
Popovic, Vesna, Atanasijevic, Tatjana, Nikolic, Slobodan, Božić, Nataša, Vujčić, Zoran, Micic-Labudovic, Jelena, "Forensic Aspects of Postmortem Serum Carbohydrate-Deficient Transferrin Analysis as a Marker of Alcohol Abuse" in Srpski arhiv za celokupno lekarstvo, 141, no. 3-4 (2013):203-206,
https://doi.org/10.2298/SARH1304203P .,
Kon_2473 .
3
3
4

The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a

Božić, Nataša; Puertas, Juan-Miguel; Lončar, Nikola L.; Sans Duran, Cristina; Lopez-Santin, Josep; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Božić, Nataša
AU  - Puertas, Juan-Miguel
AU  - Lončar, Nikola L.
AU  - Sans Duran, Cristina
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1638
AB  - In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a
VL  - 48
IS  - 3
SP  - 438
EP  - 442
DO  - 10.1016/j.procbio.2013.01.016
UR  - Kon_2469
ER  - 
@article{
author = "Božić, Nataša and Puertas, Juan-Miguel and Lončar, Nikola L. and Sans Duran, Cristina and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a",
volume = "48",
number = "3",
pages = "438-442",
doi = "10.1016/j.procbio.2013.01.016",
url = "Kon_2469"
}
Božić, N., Puertas, J., Lončar, N. L., Sans Duran, C., Lopez-Santin, J.,& Vujčić, Z.. (2013). The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 48(3), 438-442.
https://doi.org/10.1016/j.procbio.2013.01.016
Kon_2469
Božić N, Puertas J, Lončar NL, Sans Duran C, Lopez-Santin J, Vujčić Z. The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry. 2013;48(3):438-442.
doi:10.1016/j.procbio.2013.01.016
Kon_2469 .
Božić, Nataša, Puertas, Juan-Miguel, Lončar, Nikola L., Sans Duran, Cristina, Lopez-Santin, Josep, Vujčić, Zoran, "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a" in Process Biochemistry, 48, no. 3 (2013):438-442,
https://doi.org/10.1016/j.procbio.2013.01.016 .,
Kon_2469 .
9
8
10

Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization

Lončar, Nikola L.; Božić, Nataša; Lopez-Santin, Josep; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1431
AB  - One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization
VL  - 147
SP  - 177
EP  - 183
DO  - 10.1016/j.biortech.2013.08.056
UR  - Kon_2551
ER  - 
@article{
author = "Lončar, Nikola L. and Božić, Nataša and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization",
volume = "147",
pages = "177-183",
doi = "10.1016/j.biortech.2013.08.056",
url = "Kon_2551"
}
Lončar, N. L., Božić, N., Lopez-Santin, J.,& Vujčić, Z.. (2013). Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 147, 177-183.
https://doi.org/10.1016/j.biortech.2013.08.056
Kon_2551
Lončar NL, Božić N, Lopez-Santin J, Vujčić Z. Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology. 2013;147:177-183.
doi:10.1016/j.biortech.2013.08.056
Kon_2551 .
Lončar, Nikola L., Božić, Nataša, Lopez-Santin, Josep, Vujčić, Zoran, "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization" in Bioresource Technology, 147 (2013):177-183,
https://doi.org/10.1016/j.biortech.2013.08.056 .,
Kon_2551 .
54
50
56

Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition

Dojnov, Biljana; Pavlovic, Ratko; Božić, Nataša; Margetić, Aleksandra; Nenadovic, Vera; Ivanovic, Jelisaveta; Vujčić, Zoran

(Elsevier Science Inc, New York, 2013)

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Pavlovic, Ratko
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1627
AB  - The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
T1  - Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition
VL  - 164
IS  - 4
SP  - 259
EP  - 267
DO  - 10.1016/j.cbpb.2013.02.001
UR  - Kon_2458
ER  - 
@article{
author = "Dojnov, Biljana and Pavlovic, Ratko and Božić, Nataša and Margetić, Aleksandra and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2013",
abstract = "The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology",
title = "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition",
volume = "164",
number = "4",
pages = "259-267",
doi = "10.1016/j.cbpb.2013.02.001",
url = "Kon_2458"
}
Dojnov, B., Pavlovic, R., Božić, N., Margetić, A., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2013). Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 164(4), 259-267.
https://doi.org/10.1016/j.cbpb.2013.02.001
Kon_2458
Dojnov B, Pavlovic R, Božić N, Margetić A, Nenadovic V, Ivanovic J, Vujčić Z. Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2013;164(4):259-267.
doi:10.1016/j.cbpb.2013.02.001
Kon_2458 .
Dojnov, Biljana, Pavlovic, Ratko, Božić, Nataša, Margetić, Aleksandra, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 164, no. 4 (2013):259-267,
https://doi.org/10.1016/j.cbpb.2013.02.001 .,
Kon_2458 .
1
4
4
4

Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1

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

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1420
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1
VL  - 280
SP  - 599
EP  - 599
UR  - Kon_2540
ER  - 
@conference{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1",
volume = "280",
pages = "599-599",
url = "Kon_2540"
}
Lončar, N. L., Božić, N.,& Vujčić, Z.. (2013). Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 599-599.
Kon_2540
Lončar NL, Božić N, Vujčić Z. Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1. in FEBS Journal / Federation of European of Biochemical Societies. 2013;280:599-599.
Kon_2540 .
Lončar, Nikola L., Božić, Nataša, Vujčić, Zoran, "Cloning and characterization of a new dye degrading laccase from Bacillus amyloliquefaciens 12B1" in FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):599-599,
Kon_2540 .
1

Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study

Dojnov, Biljana; Vujčić, Zoran; Božić, Nataša; Margetić, Aleksandra; Vujčić, Miroslava; Nenadovic, Vera; Ivanovic, Jelisaveta

(Springer, Dordrecht, 2012)

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Vujčić, Zoran
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Vujčić, Miroslava
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1263
AB  - Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.
PB  - Springer, Dordrecht
T2  - Journal of Insect Conservation
T1  - Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study
VL  - 16
IS  - 2
SP  - 239
EP  - 247
DO  - 10.1007/s10841-011-9411-x
UR  - Kon_2286
ER  - 
@article{
author = "Dojnov, Biljana and Vujčić, Zoran and Božić, Nataša and Margetić, Aleksandra and Vujčić, Miroslava and Nenadovic, Vera and Ivanovic, Jelisaveta",
year = "2012",
abstract = "Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.",
publisher = "Springer, Dordrecht",
journal = "Journal of Insect Conservation",
title = "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study",
volume = "16",
number = "2",
pages = "239-247",
doi = "10.1007/s10841-011-9411-x",
url = "Kon_2286"
}
Dojnov, B., Vujčić, Z., Božić, N., Margetić, A., Vujčić, M., Nenadovic, V.,& Ivanovic, J.. (2012). Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation
Springer, Dordrecht., 16(2), 239-247.
https://doi.org/10.1007/s10841-011-9411-x
Kon_2286
Dojnov B, Vujčić Z, Božić N, Margetić A, Vujčić M, Nenadovic V, Ivanovic J. Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation. 2012;16(2):239-247.
doi:10.1007/s10841-011-9411-x
Kon_2286 .
Dojnov, Biljana, Vujčić, Zoran, Božić, Nataša, Margetić, Aleksandra, Vujčić, Miroslava, Nenadovic, Vera, Ivanovic, Jelisaveta, "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study" in Journal of Insect Conservation, 16, no. 2 (2012):239-247,
https://doi.org/10.1007/s10841-011-9411-x .,
Kon_2286 .
13
15
14

Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase

Lončar, Nikola L.; Božić, Nataša; Anđelković, Ivan; Milovanovic, Aleksandra; Dojnov, Biljana; Vujčić, Miroslava; Roglić, Goran; Vujčić, Zoran

(Serbian Chemical Soc, Belgrade, 2011)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Anđelković, Ivan
AU  - Milovanovic, Aleksandra
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Roglić, Goran
AU  - Vujčić, Zoran
PY  - 2011
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1339
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
UR  - Kon_2177
ER  - 
@article{
author = "Lončar, Nikola L. and Božić, Nataša and Anđelković, Ivan and Milovanovic, 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",
url = "Kon_2177"
}
Lončar, N. L., Božić, N., Anđelković, I., Milovanovic, 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
Kon_2177
Lončar NL, Božić N, Anđelković I, Milovanovic 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
Kon_2177 .
Lončar, Nikola L., Božić, Nataša, Anđelković, Ivan, Milovanovic, 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 .,
Kon_2177 .
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