TY  - JOUR
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Ðorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5165
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
T2  - Polymers
T1  - Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation
IS  - 13
SP  - 2614
VL  - 14
DO  - 10.3390/polym14132614
ER  - 

@article{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Ðorđević, 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",
journal = "Polymers",
title = "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation",
number = "13",
pages = "2614",
volume = "14",
doi = "10.3390/polym14132614"
}

Jonović, M., Jugović, B., Žuža, M., Ðorđević, 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., 14(13), 2614.
https://doi.org/10.3390/polym14132614

Jonović M, Jugović B, Žuža M, Ðorđević 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 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Ðorđević, 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 . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Milašinović, Nikola
AU  - Jonović, Marko M.
AU  - Jovanović, Jelena
AU  - Kalagasidis Krušić, Melina
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2017
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3544
AB  - In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Design and characterization of alcalase-chitosan conjugates as potential biocatalysts
EP  - 1723
IS  - 11
SP  - 1713
VL  - 40
DO  - 10.1007/s00449-017-1826-7
ER  - 

@article{
author = "Žuža, Milena and Milašinović, Nikola and Jonović, Marko M. and Jovanović, Jelena and Kalagasidis Krušić, Melina and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2017",
abstract = "In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts",
pages = "1723-1713",
number = "11",
volume = "40",
doi = "10.1007/s00449-017-1826-7"
}

Žuža, M., Milašinović, N., Jonović, M. M., Jovanović, J., Kalagasidis Krušić, M., Bugarski, B.,& Knežević-Jugović, Z.. (2017). Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering
Springer, New York., 40(11), 1713-1723.
https://doi.org/10.1007/s00449-017-1826-7

Žuža M, Milašinović N, Jonović MM, Jovanović J, Kalagasidis Krušić M, Bugarski B, Knežević-Jugović Z. Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering. 2017;40(11):1713-1723.
doi:10.1007/s00449-017-1826-7 .

Žuža, Milena, Milašinović, Nikola, Jonović, Marko M., Jovanović, Jelena, Kalagasidis Krušić, Melina, Bugarski, Branko, Knežević-Jugović, Zorica, "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts" in Bioprocess and Biosystems Engineering, 40, no. 11 (2017):1713-1723,
https://doi.org/10.1007/s00449-017-1826-7 . .