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  - 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 . .