TY  - JOUR
AU  - Popović, Nikolina
AU  - Przulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilic-Durdic, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1490
AB  - High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV-Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.
PB  - Elsevier, Amsterdam
T2  - International Journal of Biological Macromolecules
T1  - Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization
EP  - 1080
SP  - 1072
VL  - 181
DO  - 10.1016/j.ijbiomac.2021.04.115
ER  - 

@article{
author = "Popović, Nikolina and Przulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilic-Durdic, Karla and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2021",
abstract = "High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV-Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Biological Macromolecules",
title = "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization",
pages = "1080-1072",
volume = "181",
doi = "10.1016/j.ijbiomac.2021.04.115"
}

Popović, N., Przulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilic-Durdic, K., Ostafe, R., Fischer, R.,& Prodanović, R.. (2021). Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization. in International Journal of Biological Macromolecules
Elsevier, Amsterdam., 181, 1072-1080.
https://doi.org/10.1016/j.ijbiomac.2021.04.115

Popović N, Przulj D, Mladenović M, Prodanović O, Ece S, Ilic-Durdic K, Ostafe R, Fischer R, Prodanović R. Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization. in International Journal of Biological Macromolecules. 2021;181:1072-1080.
doi:10.1016/j.ijbiomac.2021.04.115 .

Popović, Nikolina, Przulj, Dunja, Mladenović, Maja, Prodanović, Olivera, Ece, Selin, Ilic-Durdic, Karla, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization" in International Journal of Biological Macromolecules, 181 (2021):1072-1080,
https://doi.org/10.1016/j.ijbiomac.2021.04.115 . .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Stanisic, Marija
AU  - Ilic-Durdic, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1484
AB  - Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV-Vis, FTIR, and H-1 NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.
PB  - Elsevier, Amsterdam
T2  - Environmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
VL  - 22
DO  - 10.1016/j.eti.2021.101399
ER  - 

@article{
author = "Popović, Nikolina and Stanisic, Marija and Ilic-Durdic, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
abstract = "Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV-Vis, FTIR, and H-1 NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.",
publisher = "Elsevier, Amsterdam",
journal = "Environmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization",
volume = "22",
doi = "10.1016/j.eti.2021.101399"
}

Popović, N., Stanisic, M., Ilic-Durdic, K., Prodanović, O., Polović, N.,& Prodanović, R.. (2021). Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation
Elsevier, Amsterdam., 22.
https://doi.org/10.1016/j.eti.2021.101399

Popović N, Stanisic M, Ilic-Durdic K, Prodanović O, Polović N, Prodanović R. Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation. 2021;22.
doi:10.1016/j.eti.2021.101399 .

Popović, Nikolina, Stanisic, Marija, Ilic-Durdic, Karla, Prodanović, Olivera, Polović, Natalija, Prodanović, Radivoje, "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization" in Environmental Technology & Innovation, 22 (2021),
https://doi.org/10.1016/j.eti.2021.101399 . .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Prodanović, Radivoje
AU  - Ilic-Durdic, Karla
AU  - Polović, Natalija
AU  - Spasojević, Milica
AU  - Prodanović, Olivera
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1476
AB  - Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the enzyme is a major issue which can be successfully overcome by the enzyme immobilization on different polymers. In this study, tyramine-alginate micro-beads were used as carriers for the immobilization of horseradish peroxidase. The effect of the oxidation degree of tyramine-alginates on a specific activity of the enzyme was tested. An increase in the concentration of oxidized alginate from 2.5 to 20% resulted in a gradual increase in the specific activity from 0.05 to 0.67 U/mL. HRP immobilized within these microbeads was tested for the phenol removal in a batch reactor. Reaction conditions were optimized to achieve a high removal efficiency and substantial reusability of the system. In this study, for the first time, an internal generation of hydrogen peroxide from glucose and glucose oxidase was employed in the phenol removal process with HRP immobilized on tyramine-alginate. Within 6 h of repeated use 96% of phenol was removed when the system for internal delivery of H2O2, composed of 0.187 U/mL of glucose oxidase and 4 mmol/L of glucose was employed. A common straightforward addition of hydrogen peroxide provided the removal efficiency of only 42%, under the same reaction conditions. The highest efficiency of the phenol removal (96%) was obtained with HRP immobilized within 20 mol% oxidized tyramine-alginate microbeads. Fifteen mol% oxidized tyramine-alginate showed lower removal efficiency in the first cycle of use (73%) but more promising reusability, since the immobilized enzyme retained 61% of its initial activity even after four consecutive cycles of use.
PB  - Elsevier, Amsterdam
T2  - Environmental Technology & Innovation
T1  - Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads
VL  - 21
DO  - 10.1016/j.eti.2020.101211
ER  - 

@article{
author = "Pantić, Nevena and Prodanović, Radivoje and Ilic-Durdic, Karla and Polović, Natalija and Spasojević, Milica and Prodanović, Olivera",
year = "2021",
abstract = "Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the enzyme is a major issue which can be successfully overcome by the enzyme immobilization on different polymers. In this study, tyramine-alginate micro-beads were used as carriers for the immobilization of horseradish peroxidase. The effect of the oxidation degree of tyramine-alginates on a specific activity of the enzyme was tested. An increase in the concentration of oxidized alginate from 2.5 to 20% resulted in a gradual increase in the specific activity from 0.05 to 0.67 U/mL. HRP immobilized within these microbeads was tested for the phenol removal in a batch reactor. Reaction conditions were optimized to achieve a high removal efficiency and substantial reusability of the system. In this study, for the first time, an internal generation of hydrogen peroxide from glucose and glucose oxidase was employed in the phenol removal process with HRP immobilized on tyramine-alginate. Within 6 h of repeated use 96% of phenol was removed when the system for internal delivery of H2O2, composed of 0.187 U/mL of glucose oxidase and 4 mmol/L of glucose was employed. A common straightforward addition of hydrogen peroxide provided the removal efficiency of only 42%, under the same reaction conditions. The highest efficiency of the phenol removal (96%) was obtained with HRP immobilized within 20 mol% oxidized tyramine-alginate microbeads. Fifteen mol% oxidized tyramine-alginate showed lower removal efficiency in the first cycle of use (73%) but more promising reusability, since the immobilized enzyme retained 61% of its initial activity even after four consecutive cycles of use.",
publisher = "Elsevier, Amsterdam",
journal = "Environmental Technology & Innovation",
title = "Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads",
volume = "21",
doi = "10.1016/j.eti.2020.101211"
}

Pantić, N., Prodanović, R., Ilic-Durdic, K., Polović, N., Spasojević, M.,& Prodanović, O.. (2021). Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads. in Environmental Technology & Innovation
Elsevier, Amsterdam., 21.
https://doi.org/10.1016/j.eti.2020.101211

Pantić N, Prodanović R, Ilic-Durdic K, Polović N, Spasojević M, Prodanović O. Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads. in Environmental Technology & Innovation. 2021;21.
doi:10.1016/j.eti.2020.101211 .

Pantić, Nevena, Prodanović, Radivoje, Ilic-Durdic, Karla, Polović, Natalija, Spasojević, Milica, Prodanović, Olivera, "Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads" in Environmental Technology & Innovation, 21 (2021),
https://doi.org/10.1016/j.eti.2020.101211 . .