Spasojević, Dragica

Link to this page

Authority KeyName Variants
95fc5bde-8f62-463b-a92a-d437335cd944
  • Spasojević, Dragica (2)
Projects

Author's Bibliography

Horseradish peroxidase immobilization within micro-beads of oxidized tyramine-alginate for phenol removal from wastewater

Surudžić, Nevena; Spasojević, Dragica; Stanković, Mira; Spasojević, Milica; Elgahwash, Reyadh Gomah Amar; Prodanović, Radivoje; Prodanović, Olivera

(University of Belgrade, Technical Faculty in Bor, 2023)

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 .

Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation

Spasojević, Dragica; Prokopijević, Miloš; Prodanović, Olivera; Zelenović, Nevena D.; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(The Polymer Society of Korea, 2019)

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 . .
5
3
4
5