TY  - DATA
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - https://dais.sanu.ac.rs/123456789/13156
AB  - Figure S1: Effects on the decolorization process: HRP-MAB size (a) AB225, (b) AV109; MAG-alginate ratio (c) AB225, (d) AV109; initial HRP concentration (e) AB225, (f) AV109; HRP-MAB mass (g) AB225, (h) AV109; initial H2O2 concentration (i) AB225, (j) AV109 and initial dye concentration (k) AB225, (l) AV109; Table S1: Reaction conditions for the optimization of decolorization process of AB225 and AV109 color
PB  - MDPI AG
T2  - Polymers
T1  - Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614
VL  - 14
UR  - https://hdl.handle.net/21.15107/rcub_dais_13156
ER  - 

@misc{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Đorđević, Verica and Milašinović, Nikola and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2022",
abstract = "Figure S1: Effects on the decolorization process: HRP-MAB size (a) AB225, (b) AV109; MAG-alginate ratio (c) AB225, (d) AV109; initial HRP concentration (e) AB225, (f) AV109; HRP-MAB mass (g) AB225, (h) AV109; initial H2O2 concentration (i) AB225, (j) AV109 and initial dye concentration (k) AB225, (l) AV109; Table S1: Reaction conditions for the optimization of decolorization process of AB225 and AV109 color",
publisher = "MDPI AG",
journal = "Polymers",
title = "Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614",
volume = "14",
url = "https://hdl.handle.net/21.15107/rcub_dais_13156"
}

Jonović, M., Jugović, B., Žuža, M., Đorđević, V., Milašinović, N., Bugarski, B.,& Knežević-Jugović, Z.. (2022). Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614. in Polymers
MDPI AG., 14.
https://hdl.handle.net/21.15107/rcub_dais_13156

Jonović M, Jugović B, Žuža M, Đorđević V, Milašinović N, Bugarski B, Knežević-Jugović Z. Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614. in Polymers. 2022;14.
https://hdl.handle.net/21.15107/rcub_dais_13156 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Supplementary information for the article Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614, https://doi.org/10.3390/polym14132614" in Polymers, 14 (2022),
https://hdl.handle.net/21.15107/rcub_dais_13156 .

TY  - JOUR
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - https://dais.sanu.ac.rs/123456789/13155
AB  - The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.
PB  - MDPI AG
T2  - Polymers
T1  - Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation
SP  - 2614
VL  - 14
IS  - 13
DO  - 10.3390/polym14132614
UR  - https://hdl.handle.net/21.15107/rcub_dais_13155
ER  - 

@article{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Đorđević, Verica and Milašinović, Nikola and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2022",
abstract = "The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.",
publisher = "MDPI AG",
journal = "Polymers",
title = "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation",
pages = "2614",
volume = "14",
number = "13",
doi = "10.3390/polym14132614",
url = "https://hdl.handle.net/21.15107/rcub_dais_13155"
}

Jonović, M., Jugović, B., Žuža, M., Đorđević, V., Milašinović, N., Bugarski, B.,& Knežević-Jugović, Z.. (2022). Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers
MDPI AG., 14(13), 2614.
https://doi.org/10.3390/polym14132614
https://hdl.handle.net/21.15107/rcub_dais_13155

Jonović M, Jugović B, Žuža M, Đorđević V, Milašinović N, Bugarski B, Knežević-Jugović Z. Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers. 2022;14(13):2614.
doi:10.3390/polym14132614
https://hdl.handle.net/21.15107/rcub_dais_13155 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Đorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614,
https://doi.org/10.3390/polym14132614 .,
https://hdl.handle.net/21.15107/rcub_dais_13155 .

TY  - JOUR
AU  - Jonović, Marko
AU  - Žuža, Milena
AU  - Đorđević, Verica
AU  - Šekuljica, Nataša
AU  - Milivojević, Milan
AU  - Jugović, Branimir
AU  - Bugarski, Branko
AU  - Knežević Jugović, Zorica
PY  - 2021
UR  - https://dais.sanu.ac.rs/123456789/12087
AB  - Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 +/- 23 mu m) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 +/- 103 nm and 394 +/- 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 +/- 4 mg g(-1) on the carrier and the highest immobilized alcalase activity of 2716.1 IU g(-1) in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.
PB  - Basel : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - catalysts
T1  - Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins
SP  - 305
VL  - 11
IS  - 3
DO  - 10.3390/catal11030305
UR  - https://hdl.handle.net/21.15107/rcub_dais_12087
ER  - 

@article{
author = "Jonović, Marko and Žuža, Milena and Đorđević, Verica and Šekuljica, Nataša and Milivojević, Milan and Jugović, Branimir and Bugarski, Branko and Knežević Jugović, Zorica",
year = "2021",
abstract = "Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 +/- 23 mu m) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 +/- 103 nm and 394 +/- 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 +/- 4 mg g(-1) on the carrier and the highest immobilized alcalase activity of 2716.1 IU g(-1) in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.",
publisher = "Basel : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "catalysts",
title = "Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins",
pages = "305",
volume = "11",
number = "3",
doi = "10.3390/catal11030305",
url = "https://hdl.handle.net/21.15107/rcub_dais_12087"
}

Jonović, M., Žuža, M., Đorđević, V., Šekuljica, N., Milivojević, M., Jugović, B., Bugarski, B.,& Knežević Jugović, Z.. (2021). Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins. in catalysts
Basel : Multidisciplinary Digital Publishing Institute (MDPI)., 11(3), 305.
https://doi.org/10.3390/catal11030305
https://hdl.handle.net/21.15107/rcub_dais_12087

Jonović M, Žuža M, Đorđević V, Šekuljica N, Milivojević M, Jugović B, Bugarski B, Knežević Jugović Z. Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins. in catalysts. 2021;11(3):305.
doi:10.3390/catal11030305
https://hdl.handle.net/21.15107/rcub_dais_12087 .

Jonović, Marko, Žuža, Milena, Đorđević, Verica, Šekuljica, Nataša, Milivojević, Milan, Jugović, Branimir, Bugarski, Branko, Knežević Jugović, Zorica, "Immobilized Alcalase on Micron- and Submicron-Sized Alginate Beads as a Potential Biocatalyst for Hydrolysis of Food Proteins" in catalysts, 11, no. 3 (2021):305,
https://doi.org/10.3390/catal11030305 .,
https://hdl.handle.net/21.15107/rcub_dais_12087 .