TY  - JOUR
AU  - Glišić, Sanja
AU  - Prodanović, Radivoje
AU  - Paessler, Slobodan
AU  - Perović, Vladimir
AU  - Milićević, Jelena
AU  - Prodanović, Olivera
AU  - Senčanski, Milan 
AU  - Kaličanin, Nevena
AU  - Protić, Sara
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5884
AB  - Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing can be an effective option for achieving a rapid response. This study used a combined in silico virtual screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking. Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro. After the expression and purification of PLpro, gramicidin D was screened for protease inhibition in vitro and was found to be active against PLpro. The current study’s findings are significant because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable safety profile.
PB  - MDPI
T2  - Int. J. Mol. Sci.
T1  - In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D
VL  - 24
IS  - 3
SP  - 1955
DO  - 10.3390/ijms24031955
ER  - 

@article{
author = "Glišić, Sanja and Prodanović, Radivoje and Paessler, Slobodan and Perović, Vladimir and Milićević, Jelena and Prodanović, Olivera and Senčanski, Milan  and Kaličanin, Nevena and Protić, Sara",
year = "2023",
abstract = "Finding an effective drug to prevent or treat COVID-19 is of utmost importance in tcurrent pandemic. Since developing a new treatment takes a significant amount of time, drug repurposing can be an effective option for achieving a rapid response. This study used a combined in silico virtual screening protocol for candidate SARS-CoV-2 PLpro inhibitors. The Drugbank database was searched first, using the Informational Spectrum Method for Small Molecules, followed by molecular docking. Gramicidin D was selected as a peptide drug, showing the best in silico interaction profile with PLpro. After the expression and purification of PLpro, gramicidin D was screened for protease inhibition in vitro and was found to be active against PLpro. The current study’s findings are significant because it is critical to identify COVID-19 therapies that are efficient, affordable, and have a favorable safety profile.",
publisher = "MDPI",
journal = "Int. J. Mol. Sci.",
title = "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D",
volume = "24",
number = "3",
pages = "1955",
doi = "10.3390/ijms24031955"
}

Glišić, S., Prodanović, R., Paessler, S., Perović, V., Milićević, J., Prodanović, O., Senčanski, M., Kaličanin, N.,& Protić, S.. (2023). In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in Int. J. Mol. Sci.
MDPI., 24(3), 1955.
https://doi.org/10.3390/ijms24031955

Glišić S, Prodanović R, Paessler S, Perović V, Milićević J, Prodanović O, Senčanski M, Kaličanin N, Protić S. In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D. in Int. J. Mol. Sci.. 2023;24(3):1955.
doi:10.3390/ijms24031955 .

Glišić, Sanja, Prodanović, Radivoje, Paessler, Slobodan, Perović, Vladimir, Milićević, Jelena, Prodanović, Olivera, Senčanski, Milan , Kaličanin, Nevena, Protić, Sara, "In Silico and In Vitro Inhibition of SARS-CoV-2 PLpro with Gramicidin D" in Int. J. Mol. Sci., 24, no. 3 (2023):1955,
https://doi.org/10.3390/ijms24031955 . .

TY  - CONF
AU  - Surudžić, Nevena
AU  - Spasojević, Dragica
AU  - Stanković, Mira
AU  - Spasojević, Milica
AU  - Elgahwash, Reyadh Gomah Amar
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6198
AB  - Natural polymers such as alginate, pectin, chitosan etc. were used as carriers for the immobilization of different types of enzymes. Among investigated enzymes, peroxidases hold a special place. Immobilized enzymes are frequently used in phenol removal reactions. In this research horseradish peroxidase was immobilized within alginate micro-beads. This natural polymer was previously oxidized with sodium periodate and modified with tyramine hydrochloride. Percent of oxidation was varied from 2.5 mol% to 10 mol%, and an increase in specific activity was noticed with increasing the oxidation percent. Immobilized peroxidases showed satisfactory stabilities after 10 days of storage. Phenol concentration in a batch reactor decreased during its oxidation with horseradish peroxidase immobilized on tyramine-alginate hydrogels.
PB  - University of Belgrade, Technical Faculty in Bor
C3  - 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
T1  - Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater
SP  - 267
EP  - 271
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2012
ER  - 

@conference{
author = "Surudžić, Nevena and Spasojević, Dragica and Stanković, Mira and Spasojević, Milica and Elgahwash, Reyadh Gomah Amar and Prodanović, Radivoje and Prodanović, Olivera",
year = "2023",
abstract = "Natural polymers such as alginate, pectin, chitosan etc. were used as carriers for the immobilization of different types of enzymes. Among investigated enzymes, peroxidases hold a special place. Immobilized enzymes are frequently used in phenol removal reactions. In this research horseradish peroxidase was immobilized within alginate micro-beads. This natural polymer was previously oxidized with sodium periodate and modified with tyramine hydrochloride. Percent of oxidation was varied from 2.5 mol% to 10 mol%, and an increase in specific activity was noticed with increasing the oxidation percent. Immobilized peroxidases showed satisfactory stabilities after 10 days of storage. Phenol concentration in a batch reactor decreased during its oxidation with horseradish peroxidase immobilized on tyramine-alginate hydrogels.",
publisher = "University of Belgrade, Technical Faculty in Bor",
journal = "30th International Conference Ecological Truth and Environmental Research – EcoTER’23",
title = "Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater",
pages = "267-271",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2012"
}

Surudžić, N., Spasojević, D., Stanković, M., Spasojević, M., Elgahwash, R. G. A., Prodanović, R.,& Prodanović, O.. (2023). Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23
University of Belgrade, Technical Faculty in Bor., 267-271.
https://hdl.handle.net/21.15107/rcub_rimsi_2012

Surudžić N, Spasojević D, Stanković M, Spasojević M, Elgahwash RGA, Prodanović R, Prodanović O. Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater. in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23. 2023;:267-271.
https://hdl.handle.net/21.15107/rcub_rimsi_2012 .

Surudžić, Nevena, Spasojević, Dragica, Stanković, Mira, Spasojević, Milica, Elgahwash, Reyadh Gomah Amar, Prodanović, Radivoje, Prodanović, Olivera, "Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater" in 30th International Conference Ecological Truth and Environmental Research – EcoTER’23 (2023):267-271,
https://hdl.handle.net/21.15107/rcub_rimsi_2012 .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Stojanović, Željko
AU  - Veljović, Đorđe
AU  - Krstić, Jugoslav
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - https://link.springer.com/article/10.1007/s10924-021-02364-3
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5205
AB  - Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.
PB  - Springer
T2  - Journal of Polymers and the Environment
T1  - Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol
VL  - 30
SP  - 3005
EP  - 3020
DO  - 10.1007/s10924-021-02364-3
ER  - 

@article{
author = "Pantić, Nevena and Spasojević, Milica and Stojanović, Željko and Veljović, Đorđe and Krstić, Jugoslav and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera",
year = "2022",
abstract = "Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.",
publisher = "Springer",
journal = "Journal of Polymers and the Environment",
title = "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol",
volume = "30",
pages = "3005-3020",
doi = "10.1007/s10924-021-02364-3"
}

Pantić, N., Spasojević, M., Stojanović, Ž., Veljović, Đ., Krstić, J., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment
Springer., 30, 3005-3020.
https://doi.org/10.1007/s10924-021-02364-3

Pantić N, Spasojević M, Stojanović Ž, Veljović Đ, Krstić J, Balaž AM, Prodanović R, Prodanović O. Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment. 2022;30:3005-3020.
doi:10.1007/s10924-021-02364-3 .

Pantić, Nevena, Spasojević, Milica, Stojanović, Željko, Veljović, Đorđe, Krstić, Jugoslav, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol" in Journal of Polymers and the Environment, 30 (2022):3005-3020,
https://doi.org/10.1007/s10924-021-02364-3 . .

TY  - JOUR
AU  - Kovačević, Gordana
AU  - Elgahwash, Reyadh Gomah Amar
AU  - Blažić, Marija
AU  - Pantić, Nevena
AU  - Prodanović, Olivera
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5979
AB  - Saccharomyces cerevisiae, known as bakers’ yeast, is one of the most utilized yeasts in industry. Several enzymes that are naturally produced by yeast, such as invertase and catalase, combined with heterologously expressed glucose oxidase (GOx), represent the enzyme machinery for fructose and gluconic acid production. Therefore, we have used yeast cell walls with expressed glucose oxidase as a platform for crosslinking with invertase and catalase to create biocatalyst cells for the high yield sucrose conversion. Using 5% (w/v) suspension of cross-linked yeast cell walls in 0.15 M sucrose solution, 1.86 g L−1 h−1 of gluconic acid has been obtained using wt-GOx, while mutant A2-GOx produced 2.91 g L−1 h−1 of gluconic acid. Increasing the concentration of modified yeast cells walls to 10% (w/v) we were able to obtain almost 100% conversion of glucose to gluconic acid using A2-GOx in the first cycle. Reusing the modified cells walls in three consecutive cycles, conversion dropped to approximately 70% using A2-GOx and 40% using wt-GOx.
PB  - Elsevier
T2  - Molecular Catalysis
T1  - Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface
VL  - 522
IS  - 112215
DO  - 10.1016/j.mcat.2022.112215
ER  - 

@article{
author = "Kovačević, Gordana and Elgahwash, Reyadh Gomah Amar and Blažić, Marija and Pantić, Nevena and Prodanović, Olivera and Balaž, Ana Marija and Prodanović, Radivoje",
year = "2022",
abstract = "Saccharomyces cerevisiae, known as bakers’ yeast, is one of the most utilized yeasts in industry. Several enzymes that are naturally produced by yeast, such as invertase and catalase, combined with heterologously expressed glucose oxidase (GOx), represent the enzyme machinery for fructose and gluconic acid production. Therefore, we have used yeast cell walls with expressed glucose oxidase as a platform for crosslinking with invertase and catalase to create biocatalyst cells for the high yield sucrose conversion. Using 5% (w/v) suspension of cross-linked yeast cell walls in 0.15 M sucrose solution, 1.86 g L−1 h−1 of gluconic acid has been obtained using wt-GOx, while mutant A2-GOx produced 2.91 g L−1 h−1 of gluconic acid. Increasing the concentration of modified yeast cells walls to 10% (w/v) we were able to obtain almost 100% conversion of glucose to gluconic acid using A2-GOx in the first cycle. Reusing the modified cells walls in three consecutive cycles, conversion dropped to approximately 70% using A2-GOx and 40% using wt-GOx.",
publisher = "Elsevier",
journal = "Molecular Catalysis",
title = "Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface",
volume = "522",
number = "112215",
doi = "10.1016/j.mcat.2022.112215"
}

Kovačević, G., Elgahwash, R. G. A., Blažić, M., Pantić, N., Prodanović, O., Balaž, A. M.,& Prodanović, R.. (2022). Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface. in Molecular Catalysis
Elsevier., 522(112215).
https://doi.org/10.1016/j.mcat.2022.112215

Kovačević G, Elgahwash RGA, Blažić M, Pantić N, Prodanović O, Balaž AM, Prodanović R. Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface. in Molecular Catalysis. 2022;522(112215).
doi:10.1016/j.mcat.2022.112215 .

Kovačević, Gordana, Elgahwash, Reyadh Gomah Amar, Blažić, Marija, Pantić, Nevena, Prodanović, Olivera, Balaž, Ana Marija, Prodanović, Radivoje, "Production of fructose and gluconic acid from sucrose with cross-linked yeast cell walls expressing glucose oxidase on the surface" in Molecular Catalysis, 522, no. 112215 (2022),
https://doi.org/10.1016/j.mcat.2022.112215 . .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Prodanović, Radivoje
AU  - Ilić Đurđić, Karla
AU  - Polović, Natalija
AU  - Spasojević, Milica
AU  - Prodanović, Olivera
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4768
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 micro-beads 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 micro-beads. 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
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads
VL  - 21
SP  - 101211
DO  - 10.1016/j.eti.2020.101211
ER  - 

@article{
author = "Pantić, Nevena and Prodanović, Radivoje and Ilić Đurđić, 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 micro-beads 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 micro-beads. 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",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads",
volume = "21",
pages = "101211",
doi = "10.1016/j.eti.2020.101211"
}

Pantić, N., Prodanović, R., Ilić Đurđić, 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., 21, 101211.
https://doi.org/10.1016/j.eti.2020.101211

Pantić N, Prodanović R, Ilić Đurđić 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;21:101211.
doi:10.1016/j.eti.2020.101211 .

Pantić, Nevena, Prodanović, Radivoje, Ilić Đurđić, 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):101211,
https://doi.org/10.1016/j.eti.2020.101211 . .

TY  - DATA
AU  - Popović, Nikolina
AU  - Stanišić, Marija D.
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4493
PB  - Elsevier
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4494
ER  - 

@misc{
author = "Popović, Nikolina and Stanišić, Marija D. and Ilić Đurđić, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
publisher = "Elsevier",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4494"
}

Popović, N., Stanišić, M. D., Ilić Đurđić, K., Prodanović, O., Polović, N.,& Prodanović, R.. (2021). Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.. in Environmental Technology & Innovation
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4494

Popović N, Stanišić MD, Ilić Đurđić K, Prodanović O, Polović N, Prodanović R. Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.. in Environmental Technology & Innovation. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4494 .

Popović, Nikolina, Stanišić, Marija D., Ilić Đurđić, Karla, Prodanović, Olivera, Polović, Natalija, Prodanović, Radivoje, "Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399." in Environmental Technology & Innovation (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4494 .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Stanišić, Marija D.
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S235218642100047X
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4493
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 1H 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
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
VL  - 22
SP  - 101399
DO  - 10.1016/j.eti.2021.101399
ER  - 

@article{
author = "Popović, Nikolina and Stanišić, Marija D. and Ilić Đurđić, 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 1H 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",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization",
volume = "22",
pages = "101399",
doi = "10.1016/j.eti.2021.101399"
}

Popović, N., Stanišić, M. D., Ilić Đurđić, 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., 22, 101399.
https://doi.org/10.1016/j.eti.2021.101399

Popović N, Stanišić MD, Ilić Đurđić 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;22:101399.
doi:10.1016/j.eti.2021.101399 .

Popović, Nikolina, Stanišić, Marija D., Ilić Đurđić, 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):101399,
https://doi.org/10.1016/j.eti.2021.101399 . .

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4101
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.
PB  - Springer
T2  - Frontiers of Environmental Science & Engineering
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls
VL  - 15
IS  - 2
SP  - 19
DO  - 10.1007/s11783-020-1311-4
ER  - 

@article{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.",
publisher = "Springer",
journal = "Frontiers of Environmental Science & Engineering, Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls",
volume = "15",
number = "2",
pages = "19",
doi = "10.1007/s11783-020-1311-4"
}

Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering
Springer., 15(2), 19.
https://doi.org/10.1007/s11783-020-1311-4

Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering. 2021;15(2):19.
doi:10.1007/s11783-020-1311-4 .

Ilić Đurđić, Karla, Ostafe, Raluca, Prodanović, Olivera, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" in Frontiers of Environmental Science & Engineering, 15, no. 2 (2021):19,
https://doi.org/10.1007/s11783-020-1311-4 . .

TY  - DATA
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4103
PB  - Springer
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4103
ER  - 

@misc{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
publisher = "Springer",
journal = "Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4103"
}

Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4. in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_4103

Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4. in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4103 .

Ilić Đurđić, Karla, Ostafe, Raluca, Prodanović, Olivera, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4" in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng. (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4103 .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Pržulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021008813
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4404
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.
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
VL  - 181
SP  - 1072
EP  - 1080
DO  - 10.1016/j.ijbiomac.2021.04.115
ER  - 

@article{
author = "Popović, Nikolina and Pržulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilić Đurđić, 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.",
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",
volume = "181",
pages = "1072-1080",
doi = "10.1016/j.ijbiomac.2021.04.115"
}

Popović, N., Pržulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilić Đurđić, 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, 181, 1072-1080.
https://doi.org/10.1016/j.ijbiomac.2021.04.115

Popović N, Pržulj D, Mladenović M, Prodanović O, Ece S, Ilić Đurđić 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, Pržulj, Dunja, Mladenović, Maja, Prodanović, Olivera, Ece, Selin, Ilić Đurđić, 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  - DATA
AU  - Popović, Nikolina
AU  - Pržulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021008813
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4405
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Popović, N.; Pržulj, D.; Mladenović, M.; Prodanović, O.; Ece, S.; Ilić Đurđić, 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. International Journal of Biological Macromolecules 2021, 181, 1072–1080. https://doi.org/10.1016/j.ijbiomac.2021.04.115.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4405
ER  - 

@misc{
author = "Popović, Nikolina and Pržulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilić Đurđić, Karla and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2021",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Popović, N.; Pržulj, D.; Mladenović, M.; Prodanović, O.; Ece, S.; Ilić Đurđić, 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. International Journal of Biological Macromolecules 2021, 181, 1072–1080. https://doi.org/10.1016/j.ijbiomac.2021.04.115.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4405"
}

Popović, N., Pržulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilić Đurđić, K., Ostafe, R., Fischer, R.,& Prodanović, R.. (2021). Supplementary data for the article: Popović, N.; Pržulj, D.; Mladenović, M.; Prodanović, O.; Ece, S.; Ilić Đurđić, 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. International Journal of Biological Macromolecules 2021, 181, 1072–1080. https://doi.org/10.1016/j.ijbiomac.2021.04.115.. in International Journal of Biological Macromolecules.
https://hdl.handle.net/21.15107/rcub_cherry_4405

Popović N, Pržulj D, Mladenović M, Prodanović O, Ece S, Ilić Đurđić K, Ostafe R, Fischer R, Prodanović R. Supplementary data for the article: Popović, N.; Pržulj, D.; Mladenović, M.; Prodanović, O.; Ece, S.; Ilić Đurđić, 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. International Journal of Biological Macromolecules 2021, 181, 1072–1080. https://doi.org/10.1016/j.ijbiomac.2021.04.115.. in International Journal of Biological Macromolecules. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4405 .

Popović, Nikolina, Pržulj, Dunja, Mladenović, Maja, Prodanović, Olivera, Ece, Selin, Ilić Đurđić, Karla, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for the article: Popović, N.; Pržulj, D.; Mladenović, M.; Prodanović, O.; Ece, S.; Ilić Đurđić, 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. International Journal of Biological Macromolecules 2021, 181, 1072–1080. https://doi.org/10.1016/j.ijbiomac.2021.04.115." in International Journal of Biological Macromolecules (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4405 .

TY  - JOUR
AU  - Popović, Nikolina
AU  - Pržulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021008813
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4406
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.
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
VL  - 181
SP  - 1072
EP  - 1080
DO  - 10.1016/j.ijbiomac.2021.04.115
ER  - 

@article{
author = "Popović, Nikolina and Pržulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilić Đurđić, 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.",
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",
volume = "181",
pages = "1072-1080",
doi = "10.1016/j.ijbiomac.2021.04.115"
}

Popović, N., Pržulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilić Đurđić, 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, 181, 1072-1080.
https://doi.org/10.1016/j.ijbiomac.2021.04.115

Popović N, Pržulj D, Mladenović M, Prodanović O, Ece S, Ilić Đurđić 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, Pržulj, Dunja, Mladenović, Maja, Prodanović, Olivera, Ece, Selin, Ilić Đurđić, 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  - Balaž, Ana Marija
AU  - Blažić, Marija
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4270
AB  - Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZα plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion- -exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s-1 for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM-1 s-1. All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.
AB  - У циљу употребе у биосензорима и биогоривним ћелијама, успостављена је производњарастворних облика целобиоза дехидрогеназе (CDH) претходно еволуираних на површиниквашчевих ћелија S. cerevisiae. У ту сврху су мутанти CDH, tm (D20N, A64T, V592M), H5(D20N, V22A, A64T, V592M) и H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S)клонирани у pPICZα плазмид и трансформисани у Pichia pastoris KM71H сој за високуекспресију у растворном облику и кинетичку карактеризацију. После 6 дана експресије подиндукцијом метанолом, мутанти су пречишћени ултрафилтрацијом, јоноизмењивачкомхроматографијом и гел-филтрацијом. SDS електрофореза је потврдила чистоћу уз присуствоједне протеинске траке молекулскe масe од 100 kDa. Кинетичка карактеризација је показалада H5 мутирани протеин поседује највећу каталитичку константу од 43,5 s-1 за лактозу, докје H9 имао највећу константу специфичности за лактозу од 132 mM-1 s-1. Сва три мутиранапротеина су имала неизмењен pH оптимум који је био у опсегу од 4,5 до 5,5. У поређењу сапретходно добијеним природним и мутантним облицима CDH протеина из Phanerochaetechrysosporium, облици приказани у овом раду имају већу активност и специфичност, што их,повезано са високом експресијом протеина у P. Pastoris, чини добрим кандидатима за упо-требу у биотехнологији за производњу лактобионске киселине и биосензора.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain
T1  - Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju
VL  - 85
IS  - 1
SP  - 25
EP  - 35
DO  - 10.2298/JSC190320058B
ER  - 

@article{
author = "Balaž, Ana Marija and Blažić, Marija and Popović, Nikolina and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZα plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion- -exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s-1 for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM-1 s-1. All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture., У циљу употребе у биосензорима и биогоривним ћелијама, успостављена је производњарастворних облика целобиоза дехидрогеназе (CDH) претходно еволуираних на површиниквашчевих ћелија S. cerevisiae. У ту сврху су мутанти CDH, tm (D20N, A64T, V592M), H5(D20N, V22A, A64T, V592M) и H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S)клонирани у pPICZα плазмид и трансформисани у Pichia pastoris KM71H сој за високуекспресију у растворном облику и кинетичку карактеризацију. После 6 дана експресије подиндукцијом метанолом, мутанти су пречишћени ултрафилтрацијом, јоноизмењивачкомхроматографијом и гел-филтрацијом. SDS електрофореза је потврдила чистоћу уз присуствоједне протеинске траке молекулскe масe од 100 kDa. Кинетичка карактеризација је показалада H5 мутирани протеин поседује највећу каталитичку константу од 43,5 s-1 за лактозу, докје H9 имао највећу константу специфичности за лактозу од 132 mM-1 s-1. Сва три мутиранапротеина су имала неизмењен pH оптимум који је био у опсегу од 4,5 до 5,5. У поређењу сапретходно добијеним природним и мутантним облицима CDH протеина из Phanerochaetechrysosporium, облици приказани у овом раду имају већу активност и специфичност, што их,повезано са високом експресијом протеина у P. Pastoris, чини добрим кандидатима за упо-требу у биотехнологији за производњу лактобионске киселине и биосензора.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain, Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju",
volume = "85",
number = "1",
pages = "25-35",
doi = "10.2298/JSC190320058B"
}

Balaž, A. M., Blažić, M., Popović, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2020). Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 85(1), 25-35.
https://doi.org/10.2298/JSC190320058B

Balaž AM, Blažić M, Popović N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society. 2020;85(1):25-35.
doi:10.2298/JSC190320058B .

Balaž, Ana Marija, Blažić, Marija, Popović, Nikolina, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain" in Journal of the Serbian Chemical Society, 85, no. 1 (2020):25-35,
https://doi.org/10.2298/JSC190320058B . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena D.
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3732
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - The Polymer Society of Korea
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
VL  - 27
IS  - 8
SP  - 764
EP  - 771
DO  - 10.1007/s13233-019-7111-7
ER  - 

@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena D. and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "The Polymer Society of Korea",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
volume = "27",
number = "8",
pages = "764-771",
doi = "10.1007/s13233-019-7111-7"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N. D., Polović, N., Radotić, K.,& Prodanović, R.. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research
The Polymer Society of Korea., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7

Spasojević D, Prokopijević M, Prodanović O, Zelenović ND, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research. 2019;27(8):764-771.
doi:10.1007/s13233-019-7111-7 .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Zelenović, Nevena D., Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" in Macromolecular Research, 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 . .

TY  - DATA
AU  - Blažić, Marija
AU  - Balaž, Ana Marija
AU  - Prodanović, Olivera
AU  - Popović, Nikolina
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2912
PB  - Applied sciences
T2  - Applied Sciences (Switzerland)
T1  - Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2912
ER  - 

@misc{
author = "Blažić, Marija and Balaž, Ana Marija and Prodanović, Olivera and Popović, Nikolina and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
publisher = "Applied sciences",
journal = "Applied Sciences (Switzerland)",
title = "Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2912"
}

Blažić, M., Balaž, A. M., Prodanović, O., Popović, N., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413. in Applied Sciences (Switzerland)
Applied sciences..
https://hdl.handle.net/21.15107/rcub_cherry_2912

Blažić M, Balaž AM, Prodanović O, Popović N, Ostafe R, Fischer R, Prodanović R. Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413. in Applied Sciences (Switzerland). 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_2912 .

Blažić, Marija, Balaž, Ana Marija, Prodanović, Olivera, Popović, Nikolina, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413" in Applied Sciences (Switzerland) (2019),
https://hdl.handle.net/21.15107/rcub_cherry_2912 .

TY  - JOUR
AU  - Tadić, Vojin
AU  - Tadić, Jovan
AU  - Milošević, Snežana
AU  - Cingel, Aleksandar
AU  - Prodanović, Olivera
AU  - Ćosić, Tatjana
AU  - Vujčić, Zoran
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2090
AB  - In this study we investigated physiological parameters of stress (enzymatic and non-enzymatic) in lettuce (Lactuca sativa L.) and its hairy roots induced by water solution of phenol. Two varieties of lettuce were examined, Ljubljanska ledenka and Nansen. Plants were grown in water with phenol concentration of 200 mgL(-1), during 10 days. We monitored activity of peroxidases, catalases, polyphenol oxidase and superoxide dismutase, as well as proline and chlorophyll content. We observed a decrease in peroxidases, and increase in activity of catalase, polyphenol oxidase and superoxide dismutase compared to control plants. The concentration of praline was constantly increasing in both lettuce varieties over the course of the experiment. We detected an increase in activity of all monitored enzymes, except polyphenol oxidases, in hairy roots. The hydroponic system provides a useful framework for studying the effect of different harmful substances and its elimination. In such a system, as used in this work for the study of physiological processes in antioxidant protection activated when plant was exposed to phenol, lettuce and its hairy roots can be viewed as tools for water remediation.
PB  - Elsevier Science Bv, Amsterdam
T2  - Scientia Horticulturae
T1  - Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2
VL  - 232
SP  - 71
EP  - 83
DO  - 10.1016/j.scienta.2017.12.024
ER  - 

@article{
author = "Tadić, Vojin and Tadić, Jovan and Milošević, Snežana and Cingel, Aleksandar and Prodanović, Olivera and Ćosić, Tatjana and Vujčić, Zoran",
year = "2018",
abstract = "In this study we investigated physiological parameters of stress (enzymatic and non-enzymatic) in lettuce (Lactuca sativa L.) and its hairy roots induced by water solution of phenol. Two varieties of lettuce were examined, Ljubljanska ledenka and Nansen. Plants were grown in water with phenol concentration of 200 mgL(-1), during 10 days. We monitored activity of peroxidases, catalases, polyphenol oxidase and superoxide dismutase, as well as proline and chlorophyll content. We observed a decrease in peroxidases, and increase in activity of catalase, polyphenol oxidase and superoxide dismutase compared to control plants. The concentration of praline was constantly increasing in both lettuce varieties over the course of the experiment. We detected an increase in activity of all monitored enzymes, except polyphenol oxidases, in hairy roots. The hydroponic system provides a useful framework for studying the effect of different harmful substances and its elimination. In such a system, as used in this work for the study of physiological processes in antioxidant protection activated when plant was exposed to phenol, lettuce and its hairy roots can be viewed as tools for water remediation.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Scientia Horticulturae",
title = "Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2",
volume = "232",
pages = "71-83",
doi = "10.1016/j.scienta.2017.12.024"
}

Tadić, V., Tadić, J., Milošević, S., Cingel, A., Prodanović, O., Ćosić, T.,& Vujčić, Z.. (2018). Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2. in Scientia Horticulturae
Elsevier Science Bv, Amsterdam., 232, 71-83.
https://doi.org/10.1016/j.scienta.2017.12.024

Tadić V, Tadić J, Milošević S, Cingel A, Prodanović O, Ćosić T, Vujčić Z. Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2. in Scientia Horticulturae. 2018;232:71-83.
doi:10.1016/j.scienta.2017.12.024 .

Tadić, Vojin, Tadić, Jovan, Milošević, Snežana, Cingel, Aleksandar, Prodanović, Olivera, Ćosić, Tatjana, Vujčić, Zoran, "Phenol induced physiological stress in hydroponically grown lettuce (Lactuca sativa L.)- Part 2" in Scientia Horticulturae, 232 (2018):71-83,
https://doi.org/10.1016/j.scienta.2017.12.024 . .

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Kovačević, Gordana
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2421
AB  - Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization
VL  - 101
IS  - 6
SP  - 2281
EP  - 2290
DO  - 10.1007/s00253-016-8002-x
ER  - 

@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Kovačević, Gordana and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2017",
abstract = "Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization",
volume = "101",
number = "6",
pages = "2281-2290",
doi = "10.1007/s00253-016-8002-x"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Kovačević, G., Polović, N., Radotić, K.,& Prodanović, R.. (2017). Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology
Springer, New York., 101(6), 2281-2290.
https://doi.org/10.1007/s00253-016-8002-x

Prokopijević M, Prodanović O, Spasojević D, Kovačević G, Polović N, Radotić K, Prodanović R. Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology. 2017;101(6):2281-2290.
doi:10.1007/s00253-016-8002-x .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Kovačević, Gordana, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization" in Applied Microbiology and Biotechnology, 101, no. 6 (2017):2281-2290,
https://doi.org/10.1007/s00253-016-8002-x . .

TY  - DATA
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Kovačević, Gordana
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3053
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3053
ER  - 

@misc{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Kovačević, Gordana and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2017",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3053"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Kovačević, G., Polović, N., Radotić, K.,& Prodanović, R.. (2017). Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x. in Applied Microbiology and Biotechnology
Springer, New York..
https://hdl.handle.net/21.15107/rcub_cherry_3053

Prokopijević M, Prodanović O, Spasojević D, Kovačević G, Polović N, Radotić K, Prodanović R. Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x. in Applied Microbiology and Biotechnology. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3053 .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Kovačević, Gordana, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x" in Applied Microbiology and Biotechnology (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3053 .

TY  - DATA
AU  - Đokić, Lidija
AU  - Spasić, Jelena
AU  - Jeremić, Sanja
AU  - Vasiljević, Branka
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
AU  - Nikodinović-Runić, Jasmina
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3377
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Supplementary data for article: Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J. Immobilization of Escherichia Coli Cells Expressing 4-Oxalocrotonate Tautomerase for Improved Biotransformation of β-Nitrostyrene. Bioprocess and biosystems engineering 2015, 38 (12), 2389–2395. https://doi.org/10.1007/s00449-015-1474-8
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3377
ER  - 

@misc{
author = "Đokić, Lidija and Spasić, Jelena and Jeremić, Sanja and Vasiljević, Branka and Prodanović, Olivera and Prodanović, Radivoje and Nikodinović-Runić, Jasmina",
year = "2015",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Supplementary data for article: Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J. Immobilization of Escherichia Coli Cells Expressing 4-Oxalocrotonate Tautomerase for Improved Biotransformation of β-Nitrostyrene. Bioprocess and biosystems engineering 2015, 38 (12), 2389–2395. https://doi.org/10.1007/s00449-015-1474-8",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3377"
}

Đokić, L., Spasić, J., Jeremić, S., Vasiljević, B., Prodanović, O., Prodanović, R.,& Nikodinović-Runić, J.. (2015). Supplementary data for article: Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J. Immobilization of Escherichia Coli Cells Expressing 4-Oxalocrotonate Tautomerase for Improved Biotransformation of β-Nitrostyrene. Bioprocess and biosystems engineering 2015, 38 (12), 2389–2395. https://doi.org/10.1007/s00449-015-1474-8. in Bioprocess and Biosystems Engineering
Springer, New York..
https://hdl.handle.net/21.15107/rcub_cherry_3377

Đokić L, Spasić J, Jeremić S, Vasiljević B, Prodanović O, Prodanović R, Nikodinović-Runić J. Supplementary data for article: Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J. Immobilization of Escherichia Coli Cells Expressing 4-Oxalocrotonate Tautomerase for Improved Biotransformation of β-Nitrostyrene. Bioprocess and biosystems engineering 2015, 38 (12), 2389–2395. https://doi.org/10.1007/s00449-015-1474-8. in Bioprocess and Biosystems Engineering. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3377 .

Đokić, Lidija, Spasić, Jelena, Jeremić, Sanja, Vasiljević, Branka, Prodanović, Olivera, Prodanović, Radivoje, Nikodinović-Runić, Jasmina, "Supplementary data for article: Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J. Immobilization of Escherichia Coli Cells Expressing 4-Oxalocrotonate Tautomerase for Improved Biotransformation of β-Nitrostyrene. Bioprocess and biosystems engineering 2015, 38 (12), 2389–2395. https://doi.org/10.1007/s00449-015-1474-8" in Bioprocess and Biosystems Engineering (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3377 .

TY  - JOUR
AU  - Đokić, Lidija
AU  - Spasić, Jelena
AU  - Jeremić, Sanja
AU  - Vasiljević, Branka
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
AU  - Nikodinović-Runić, Jasmina
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1990
AB  - The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene
VL  - 38
IS  - 12
SP  - 2389
EP  - 2395
DO  - 10.1007/s00449-015-1474-8
ER  - 

@article{
author = "Đokić, Lidija and Spasić, Jelena and Jeremić, Sanja and Vasiljević, Branka and Prodanović, Olivera and Prodanović, Radivoje and Nikodinović-Runić, Jasmina",
year = "2015",
abstract = "The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene",
volume = "38",
number = "12",
pages = "2389-2395",
doi = "10.1007/s00449-015-1474-8"
}

Đokić, L., Spasić, J., Jeremić, S., Vasiljević, B., Prodanović, O., Prodanović, R.,& Nikodinović-Runić, J.. (2015). Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering
Springer, New York., 38(12), 2389-2395.
https://doi.org/10.1007/s00449-015-1474-8

Đokić L, Spasić J, Jeremić S, Vasiljević B, Prodanović O, Prodanović R, Nikodinović-Runić J. Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering. 2015;38(12):2389-2395.
doi:10.1007/s00449-015-1474-8 .

Đokić, Lidija, Spasić, Jelena, Jeremić, Sanja, Vasiljević, Branka, Prodanović, Olivera, Prodanović, Radivoje, Nikodinović-Runić, Jasmina, "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene" in Bioprocess and Biosystems Engineering, 38, no. 12 (2015):2389-2395,
https://doi.org/10.1007/s00449-015-1474-8 . .

TY  - DATA
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Radotić, Ksenija
AU  - Marković, Nevena
AU  - Blažić, Marija
AU  - Prodanović, Radivoje
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3457
PB  - Elsevier Science Bv, Amsterdam
T2  - Reactive and Functional Polymers
T1  - Supplementary data for article: Prodanović, O.; Spasojević, D.; Prokopijević, M.; Radotić, K.; Markovic, N.; Blažić, M.; Prodanović, R. Tyramine Modified Alginates via Periodate Oxidation for Peroxidase Induced Hydrogel Formation and Immobilization. Reactive and Functional Polymers 2015, 93, 77–83. https://doi.org/10.1016/j.reactfunctpolym.2015.06.004
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3457
ER  - 

@misc{
author = "Prodanović, Olivera and Spasojević, Dragica and Prokopijević, Miloš and Radotić, Ksenija and Marković, Nevena and Blažić, Marija and Prodanović, Radivoje",
year = "2015",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Reactive and Functional Polymers",
title = "Supplementary data for article: Prodanović, O.; Spasojević, D.; Prokopijević, M.; Radotić, K.; Markovic, N.; Blažić, M.; Prodanović, R. Tyramine Modified Alginates via Periodate Oxidation for Peroxidase Induced Hydrogel Formation and Immobilization. Reactive and Functional Polymers 2015, 93, 77–83. https://doi.org/10.1016/j.reactfunctpolym.2015.06.004",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3457"
}

Prodanović, O., Spasojević, D., Prokopijević, M., Radotić, K., Marković, N., Blažić, M.,& Prodanović, R.. (2015). Supplementary data for article: Prodanović, O.; Spasojević, D.; Prokopijević, M.; Radotić, K.; Markovic, N.; Blažić, M.; Prodanović, R. Tyramine Modified Alginates via Periodate Oxidation for Peroxidase Induced Hydrogel Formation and Immobilization. Reactive and Functional Polymers 2015, 93, 77–83. https://doi.org/10.1016/j.reactfunctpolym.2015.06.004. in Reactive and Functional Polymers
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3457

Prodanović O, Spasojević D, Prokopijević M, Radotić K, Marković N, Blažić M, Prodanović R. Supplementary data for article: Prodanović, O.; Spasojević, D.; Prokopijević, M.; Radotić, K.; Markovic, N.; Blažić, M.; Prodanović, R. Tyramine Modified Alginates via Periodate Oxidation for Peroxidase Induced Hydrogel Formation and Immobilization. Reactive and Functional Polymers 2015, 93, 77–83. https://doi.org/10.1016/j.reactfunctpolym.2015.06.004. in Reactive and Functional Polymers. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3457 .

Prodanović, Olivera, Spasojević, Dragica, Prokopijević, Miloš, Radotić, Ksenija, Marković, Nevena, Blažić, Marija, Prodanović, Radivoje, "Supplementary data for article: Prodanović, O.; Spasojević, D.; Prokopijević, M.; Radotić, K.; Markovic, N.; Blažić, M.; Prodanović, R. Tyramine Modified Alginates via Periodate Oxidation for Peroxidase Induced Hydrogel Formation and Immobilization. Reactive and Functional Polymers 2015, 93, 77–83. https://doi.org/10.1016/j.reactfunctpolym.2015.06.004" in Reactive and Functional Polymers (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3457 .

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Radotić, Ksenija
AU  - Marković, Nevena
AU  - Blažić, Marija
AU  - Prodanović, Radivoje
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1966
AB  - Phenol and amino groups were introduced into alginate to different degrees via oxidation with 2.5, 5, 10, 15 and 20 mol% of periodate and reductive amination by tyramine. Modification of alginate with tyramine was confirmed by FTIR spectroscopy and UV-VIS spectroscopy, while concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid-base titration. All tyramine-alginates were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. Tyramine-alginates oxidized with up to 10 mol% of periodate were also capable of forming hydrogels with calcium ions. Tyramine-alginates were tested for HRP immobilization within micro-beads obtained by peroxidase catalyzed droplet polymerization using internal delivery of hydrogen peroxide via glucose oxidase and glucose. Highest activity of immobilized peroxidase was obtained with 20% (w/v) tyramine-alginate obtained via 20 mol% periodate oxidation. Immobilized enzyme was not leaking from the micro-beads and was further kinetically characterized for pyrogallol oxidation. Km for pyrogallol was increased after immobilization from 1.93 mM for soluble HRP to 734 mM for immobilized HRP. The optimum pH was also increased from pH 7.0 to 8.0. Temperature and organic solvent stability improved significantly after immobilization, so that half-life at 70 degrees C increased around four times, while half-life in 80% (v/v) dioxane increased 22 times. After repeated use of 6 times in batch reactor for pyrogallol oxidation immobilized HRP retained 45% of original activity.
PB  - Elsevier Science Bv, Amsterdam
T2  - Reactive and Functional Polymers
T1  - Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization
VL  - 93
SP  - 77
EP  - 83
DO  - 10.1016/j.reactfunctpolym.2015.06.004
ER  - 

@article{
author = "Prodanović, Olivera and Spasojević, Dragica and Prokopijević, Miloš and Radotić, Ksenija and Marković, Nevena and Blažić, Marija and Prodanović, Radivoje",
year = "2015",
abstract = "Phenol and amino groups were introduced into alginate to different degrees via oxidation with 2.5, 5, 10, 15 and 20 mol% of periodate and reductive amination by tyramine. Modification of alginate with tyramine was confirmed by FTIR spectroscopy and UV-VIS spectroscopy, while concentration of phenol and ionizable groups was determined using absorbance at 275 nm and acid-base titration. All tyramine-alginates were able to form hydrogels after cross-linking with horse radish peroxidase (HRP) and hydrogen peroxide. Tyramine-alginates oxidized with up to 10 mol% of periodate were also capable of forming hydrogels with calcium ions. Tyramine-alginates were tested for HRP immobilization within micro-beads obtained by peroxidase catalyzed droplet polymerization using internal delivery of hydrogen peroxide via glucose oxidase and glucose. Highest activity of immobilized peroxidase was obtained with 20% (w/v) tyramine-alginate obtained via 20 mol% periodate oxidation. Immobilized enzyme was not leaking from the micro-beads and was further kinetically characterized for pyrogallol oxidation. Km for pyrogallol was increased after immobilization from 1.93 mM for soluble HRP to 734 mM for immobilized HRP. The optimum pH was also increased from pH 7.0 to 8.0. Temperature and organic solvent stability improved significantly after immobilization, so that half-life at 70 degrees C increased around four times, while half-life in 80% (v/v) dioxane increased 22 times. After repeated use of 6 times in batch reactor for pyrogallol oxidation immobilized HRP retained 45% of original activity.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Reactive and Functional Polymers",
title = "Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization",
volume = "93",
pages = "77-83",
doi = "10.1016/j.reactfunctpolym.2015.06.004"
}

Prodanović, O., Spasojević, D., Prokopijević, M., Radotić, K., Marković, N., Blažić, M.,& Prodanović, R.. (2015). Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization. in Reactive and Functional Polymers
Elsevier Science Bv, Amsterdam., 93, 77-83.
https://doi.org/10.1016/j.reactfunctpolym.2015.06.004

Prodanović O, Spasojević D, Prokopijević M, Radotić K, Marković N, Blažić M, Prodanović R. Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization. in Reactive and Functional Polymers. 2015;93:77-83.
doi:10.1016/j.reactfunctpolym.2015.06.004 .

Prodanović, Olivera, Spasojević, Dragica, Prokopijević, Miloš, Radotić, Ksenija, Marković, Nevena, Blažić, Marija, Prodanović, Radivoje, "Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization" in Reactive and Functional Polymers, 93 (2015):77-83,
https://doi.org/10.1016/j.reactfunctpolym.2015.06.004 . .

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1768
AB  - Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics
VL  - 37
IS  - 5
SP  - 799
EP  - 804
DO  - 10.1007/s00449-013-1050-z
ER  - 

@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Prodanović, Radivoje",
year = "2014",
abstract = "Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics",
volume = "37",
number = "5",
pages = "799-804",
doi = "10.1007/s00449-013-1050-z"
}

Prokopijević, M., Prodanović, O., Spasojević, D., Stojanović, Ž., Radotić, K.,& Prodanović, R.. (2014). Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering
Springer, New York., 37(5), 799-804.
https://doi.org/10.1007/s00449-013-1050-z

Prokopijević M, Prodanović O, Spasojević D, Stojanović Ž, Radotić K, Prodanović R. Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. in Bioprocess and Biosystems Engineering. 2014;37(5):799-804.
doi:10.1007/s00449-013-1050-z .

Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Prodanović, Radivoje, "Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics" in Bioprocess and Biosystems Engineering, 37, no. 5 (2014):799-804,
https://doi.org/10.1007/s00449-013-1050-z . .

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Pirtea, Marilen Gabriel
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1770
AB  - Immobilization of horseradish peroxidase (HRP) within alginate beads was enabled by chemical modification of the enzyme and polysaccharide chains. HRP and alginate were oxidized by periodate and subsequently modified with ethylenediamine. Highest specific activity of 0.43 U/ml of gel and 81% of bound enzyme activity was obtained using aminated HRP and alginate oxidized by periodate. Immobilized enzyme retained 75% of its original activity after 2 days of incubation in 80% (v/v) dioxane and had increased activity in basic solutions compared to native enzyme. During repeated use in batch reactor for pyrogallol oxidation immobilized peroxidase retained 75% of its original activity.
AB  - Imobilizacija peroksidaze iz rena unutar alginatnih kuglica je poboljšana hemijskom modifikacijom enzima i polisaharidnih lanaca. Peroksidaza i alginat su oksidovani perjodatom i naknadno modifikovani etilendiaminom. Najveća specifična aktivnost od 0,43 U/ml gela i 81% vezane aktivnosti je dobijeno korišćenjem aminovane peroksidaze i alginata oksidovanog perjodatom. Imobilizovani enzim je zadržao 75% originalne aktivnosti nakon 2 dana inkubacije u 80% (v/v) dioksanu i imao je povećanu aktivnost pri baznim pH vrednostima u poređenju sa nativnim enzimom. Tokom višestruke upotrebe u šaržnom reaktoru za oksidaciju pirogalola imobilizovana peroksidaza je zadržala 75% početne aktivnosti.
PB  - Assoc Chemical Engineers Serbia, Belgrade
T2  - Hemijska industrija
T1  - Immobilization of chemically modified horseradish peroxidase within activated alginate beads
T1  - Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica
VL  - 68
IS  - 1
SP  - 117
EP  - 122
DO  - 10.2298/HEMIND121122036S
ER  - 

@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Pirtea, Marilen Gabriel and Radotić, Ksenija and Prodanović, Radivoje",
year = "2014",
abstract = "Immobilization of horseradish peroxidase (HRP) within alginate beads was enabled by chemical modification of the enzyme and polysaccharide chains. HRP and alginate were oxidized by periodate and subsequently modified with ethylenediamine. Highest specific activity of 0.43 U/ml of gel and 81% of bound enzyme activity was obtained using aminated HRP and alginate oxidized by periodate. Immobilized enzyme retained 75% of its original activity after 2 days of incubation in 80% (v/v) dioxane and had increased activity in basic solutions compared to native enzyme. During repeated use in batch reactor for pyrogallol oxidation immobilized peroxidase retained 75% of its original activity., Imobilizacija peroksidaze iz rena unutar alginatnih kuglica je poboljšana hemijskom modifikacijom enzima i polisaharidnih lanaca. Peroksidaza i alginat su oksidovani perjodatom i naknadno modifikovani etilendiaminom. Najveća specifična aktivnost od 0,43 U/ml gela i 81% vezane aktivnosti je dobijeno korišćenjem aminovane peroksidaze i alginata oksidovanog perjodatom. Imobilizovani enzim je zadržao 75% originalne aktivnosti nakon 2 dana inkubacije u 80% (v/v) dioksanu i imao je povećanu aktivnost pri baznim pH vrednostima u poređenju sa nativnim enzimom. Tokom višestruke upotrebe u šaržnom reaktoru za oksidaciju pirogalola imobilizovana peroksidaza je zadržala 75% početne aktivnosti.",
publisher = "Assoc Chemical Engineers Serbia, Belgrade",
journal = "Hemijska industrija",
title = "Immobilization of chemically modified horseradish peroxidase within activated alginate beads, Imobilizacija hemijski modifikovane peroksidaze iz rena unutar aktiviranih alginatnih kuglica",
volume = "68",
number = "1",
pages = "117-122",
doi = "10.2298/HEMIND121122036S"
}

Spasojević, D., Prokopijević, M., Prodanović, O., Pirtea, M. G., Radotić, K.,& Prodanović, R.. (2014). Immobilization of chemically modified horseradish peroxidase within activated alginate beads. in Hemijska industrija
Assoc Chemical Engineers Serbia, Belgrade., 68(1), 117-122.
https://doi.org/10.2298/HEMIND121122036S

Spasojević D, Prokopijević M, Prodanović O, Pirtea MG, Radotić K, Prodanović R. Immobilization of chemically modified horseradish peroxidase within activated alginate beads. in Hemijska industrija. 2014;68(1):117-122.
doi:10.2298/HEMIND121122036S .

Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Pirtea, Marilen Gabriel, Radotić, Ksenija, Prodanović, Radivoje, "Immobilization of chemically modified horseradish peroxidase within activated alginate beads" in Hemijska industrija, 68, no. 1 (2014):117-122,
https://doi.org/10.2298/HEMIND121122036S . .

TY  - DATA
AU  - Blažić, Marija
AU  - Kovačević, Gordana
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Gavrović-Jankulović, Marija
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3568
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Protein Expression and Purification
T1  - Supplementary data for article: Blažić, M.; Kovačević, G.; Prodanović, O.; Ostafe, R.; Gavrović-Jankulović, M.; Fischer, R.; Prodanović, R. Yeast Surface Display for the Expression, Purification and Characterization of Wild-Type and B11 Mutant Glucose Oxidases. Protein Expression and Purification 2013, 89 (2), 175–180. https://doi.org/10.1016/j.pep.2013.03.014
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3568
ER  - 

@misc{
author = "Blažić, Marija and Kovačević, Gordana and Prodanović, Olivera and Ostafe, Raluca and Gavrović-Jankulović, Marija and Fischer, Rainer and Prodanović, Radivoje",
year = "2013",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Protein Expression and Purification",
title = "Supplementary data for article: Blažić, M.; Kovačević, G.; Prodanović, O.; Ostafe, R.; Gavrović-Jankulović, M.; Fischer, R.; Prodanović, R. Yeast Surface Display for the Expression, Purification and Characterization of Wild-Type and B11 Mutant Glucose Oxidases. Protein Expression and Purification 2013, 89 (2), 175–180. https://doi.org/10.1016/j.pep.2013.03.014",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3568"
}

Blažić, M., Kovačević, G., Prodanović, O., Ostafe, R., Gavrović-Jankulović, M., Fischer, R.,& Prodanović, R.. (2013). Supplementary data for article: Blažić, M.; Kovačević, G.; Prodanović, O.; Ostafe, R.; Gavrović-Jankulović, M.; Fischer, R.; Prodanović, R. Yeast Surface Display for the Expression, Purification and Characterization of Wild-Type and B11 Mutant Glucose Oxidases. Protein Expression and Purification 2013, 89 (2), 175–180. https://doi.org/10.1016/j.pep.2013.03.014. in Protein Expression and Purification
Academic Press Inc Elsevier Science, San Diego..
https://hdl.handle.net/21.15107/rcub_cherry_3568

Blažić M, Kovačević G, Prodanović O, Ostafe R, Gavrović-Jankulović M, Fischer R, Prodanović R. Supplementary data for article: Blažić, M.; Kovačević, G.; Prodanović, O.; Ostafe, R.; Gavrović-Jankulović, M.; Fischer, R.; Prodanović, R. Yeast Surface Display for the Expression, Purification and Characterization of Wild-Type and B11 Mutant Glucose Oxidases. Protein Expression and Purification 2013, 89 (2), 175–180. https://doi.org/10.1016/j.pep.2013.03.014. in Protein Expression and Purification. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3568 .

Blažić, Marija, Kovačević, Gordana, Prodanović, Olivera, Ostafe, Raluca, Gavrović-Jankulović, Marija, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for article: Blažić, M.; Kovačević, G.; Prodanović, O.; Ostafe, R.; Gavrović-Jankulović, M.; Fischer, R.; Prodanović, R. Yeast Surface Display for the Expression, Purification and Characterization of Wild-Type and B11 Mutant Glucose Oxidases. Protein Expression and Purification 2013, 89 (2), 175–180. https://doi.org/10.1016/j.pep.2013.03.014" in Protein Expression and Purification (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3568 .