Spasojević, Dragica

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  • Spasojević, Dragica (11)

Author's Bibliography

Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis

Stanković, M.; Bartolić, D.; Šikoparija, Branko; Spasojević, Dragica; Mutavdžić, Dragosav; Natić, Maja; Radotić, Ksenija

(2019)

TY  - JOUR
AU  - Stanković, M.
AU  - Bartolić, D.
AU  - Šikoparija, Branko
AU  - Spasojević, Dragica
AU  - Mutavdžić, Dragosav
AU  - Natić, Maja
AU  - Radotić, Ksenija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3115
AB  - It has been explored to what extent the ratio of the two main fluorophores in honey, originating from proteins and phenolic compounds, change between the honey extraction stage and packaging in the jars. Fluorescence spectroscopy combined with multivariate curve resolution–alternating least squares (MCR–ALS) was used to determine the ratio of the spectral components originating from phenol and proteins (Ph/Pr) fl , as a ratiometric indicator of variability in selected Lime tree (Tilia L.) honey samples. Spectrophotometric quantification of phenols and proteins in the honey samples was also performed and their ratio (Ph/Pr) sp was calculated. The values of the (Ph/Pr) fl ratio and honey protein content after packaging depended on the quality of homogenization before packaging in jars. Colorimetric and fluorometric results for phenols and proteins were in compliance. The examples are the values 3.34, 3.30, and 9, 3.14 for (Ph/Pr) fl and corresponding values 2.64, 2.18, and 12.75, 2.31 for (Ph/Pr) sp , in all pairs, the first value presenting the sample after extraction and the second value the sample after packaging in jars. Both methods show that in the former case there is no change in the phenol/protein ratio, and in the latter case the ratio decreased.
T2  - Journal of Applied Spectroscopy
T1  - Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis
VL  - 86
IS  - 2
SP  - 256
EP  - 263
DO  - 10.1007/s10812-019-00809-1
ER  - 
@article{
author = "Stanković, M. and Bartolić, D. and Šikoparija, Branko and Spasojević, Dragica and Mutavdžić, Dragosav and Natić, Maja and Radotić, Ksenija",
year = "2019",
abstract = "It has been explored to what extent the ratio of the two main fluorophores in honey, originating from proteins and phenolic compounds, change between the honey extraction stage and packaging in the jars. Fluorescence spectroscopy combined with multivariate curve resolution–alternating least squares (MCR–ALS) was used to determine the ratio of the spectral components originating from phenol and proteins (Ph/Pr) fl , as a ratiometric indicator of variability in selected Lime tree (Tilia L.) honey samples. Spectrophotometric quantification of phenols and proteins in the honey samples was also performed and their ratio (Ph/Pr) sp was calculated. The values of the (Ph/Pr) fl ratio and honey protein content after packaging depended on the quality of homogenization before packaging in jars. Colorimetric and fluorometric results for phenols and proteins were in compliance. The examples are the values 3.34, 3.30, and 9, 3.14 for (Ph/Pr) fl and corresponding values 2.64, 2.18, and 12.75, 2.31 for (Ph/Pr) sp , in all pairs, the first value presenting the sample after extraction and the second value the sample after packaging in jars. Both methods show that in the former case there is no change in the phenol/protein ratio, and in the latter case the ratio decreased.",
journal = "Journal of Applied Spectroscopy",
title = "Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis",
volume = "86",
number = "2",
pages = "256-263",
doi = "10.1007/s10812-019-00809-1"
}
Stanković, M., Bartolić, D., Šikoparija, B., Spasojević, D., Mutavdžić, D., Natić, M.,& Radotić, K.. (2019). Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis. in Journal of Applied Spectroscopy, 86(2), 256-263.
https://doi.org/10.1007/s10812-019-00809-1
Stanković M, Bartolić D, Šikoparija B, Spasojević D, Mutavdžić D, Natić M, Radotić K. Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis. in Journal of Applied Spectroscopy. 2019;86(2):256-263.
doi:10.1007/s10812-019-00809-1 .
Stanković, M., Bartolić, D., Šikoparija, Branko, Spasojević, Dragica, Mutavdžić, Dragosav, Natić, Maja, Radotić, Ksenija, "Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis" in Journal of Applied Spectroscopy, 86, no. 2 (2019):256-263,
https://doi.org/10.1007/s10812-019-00809-1 . .
3
3
2

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

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Kovačević, Gordana; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2017)

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  - http://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
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"
}
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..
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;..
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).

Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova

Spasojević, Dragica

(Универзитет у Београду, Хемијски факултет, 2017)

TY  - THES
AU  - Spasojević, Dragica
PY  - 2017
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=5601
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:17126/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=49846543
UR  - http://nardus.mpn.gov.rs/123456789/9180
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2751
AB  - Polisaharidi biljnog ćelijskog zida nalaze se u prirodi u velikim količinama, relativno su jeftini i lako dostupni i stoga predstavljaju odličan polazni izvor za sintezu novih materijala i proizvodnju hidrogelova za imobilizaciju enzima i lekova...
AB  - Polysaccharides from plant cell wall are found in nature in large quantities, they are relatively cheap and readily available, and therefore present an excellent source of starting material for the synthesis and production of new hydrogels for immobilization of enzymes and drugs...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova
ER  - 
@phdthesis{
author = "Spasojević, Dragica",
year = "2017",
abstract = "Polisaharidi biljnog ćelijskog zida nalaze se u prirodi u velikim količinama, relativno su jeftini i lako dostupni i stoga predstavljaju odličan polazni izvor za sintezu novih materijala i proizvodnju hidrogelova za imobilizaciju enzima i lekova..., Polysaccharides from plant cell wall are found in nature in large quantities, they are relatively cheap and readily available, and therefore present an excellent source of starting material for the synthesis and production of new hydrogels for immobilization of enzymes and drugs...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova"
}
Spasojević, D.. (2017). Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Spasojević D. Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova. in Универзитет у Београду. 2017;..
Spasojević, Dragica, "Modifikacija alginata, celuloze i ksilana iz ćelijskog zida biljaka, fenolnim jedinjenjima i aminima, za dobijanje hidrogelova" in Универзитет у Београду (2017).

Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Kovačević, Gordana; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2017)

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  - http://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
UR  - Kon_3237
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",
url = "Kon_3237"
}
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
Kon_3237
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
Kon_3237 .
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 .,
Kon_3237 .
8
6
7

Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014

Spasojević, Dragica; Zmejkoski, Danica; Glamoclija, Jasmina; Nikolić, Miloš; Soković, Marina; Milošević, Verica; Jarić, Ivana; Stojanović, Marijana M.; Marinković, Emilija; Barisani-Asenbauer, Talin; Prodanović, Radivoje; Jovanović, Miloš; Radotić, Ksenija

(Elsevier Science Bv, Amsterdam, 2016)

TY  - DATA
AU  - Spasojević, Dragica
AU  - Zmejkoski, Danica
AU  - Glamoclija, Jasmina
AU  - Nikolić, Miloš
AU  - Soković, Marina
AU  - Milošević, Verica
AU  - Jarić, Ivana
AU  - Stojanović, Marijana M.
AU  - Marinković, Emilija
AU  - Barisani-Asenbauer, Talin
AU  - Prodanović, Radivoje
AU  - Jovanović, Miloš
AU  - Radotić, Ksenija
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3560
PB  - Elsevier Science Bv, Amsterdam
T2  - International Journal of Antimicrobial Agents
T1  - Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014
ER  - 
@misc{
author = "Spasojević, Dragica and Zmejkoski, Danica and Glamoclija, Jasmina and Nikolić, Miloš and Soković, Marina and Milošević, Verica and Jarić, Ivana and Stojanović, Marijana M. and Marinković, Emilija and Barisani-Asenbauer, Talin and Prodanović, Radivoje and Jovanović, Miloš and Radotić, Ksenija",
year = "2016",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "International Journal of Antimicrobial Agents",
title = "Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014"
}
Spasojević, D., Zmejkoski, D., Glamoclija, J., Nikolić, M., Soković, M., Milošević, V., Jarić, I., Stojanović, M. M., Marinković, E., Barisani-Asenbauer, T., Prodanović, R., Jovanović, M.,& Radotić, K.. (2016). Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014. in International Journal of Antimicrobial Agents
Elsevier Science Bv, Amsterdam..
Spasojević D, Zmejkoski D, Glamoclija J, Nikolić M, Soković M, Milošević V, Jarić I, Stojanović MM, Marinković E, Barisani-Asenbauer T, Prodanović R, Jovanović M, Radotić K. Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014. in International Journal of Antimicrobial Agents. 2016;..
Spasojević, Dragica, Zmejkoski, Danica, Glamoclija, Jasmina, Nikolić, Miloš, Soković, Marina, Milošević, Verica, Jarić, Ivana, Stojanović, Marijana M., Marinković, Emilija, Barisani-Asenbauer, Talin, Prodanović, Radivoje, Jovanović, Miloš, Radotić, Ksenija, "Supplementary data for the article: Spasojević, D.; Zmejkoski, D.; Glamočlija, J.; Nikolić, M.; Soković, M.; Milošević, V.; Jarić, I.; Stojanović, M.; Marinković, E.; Barisani-Asenbauer, T.; et al. Lignin Model Compound in Alginate Hydrogel: A Strong Antimicrobial Agent with High Potential in Wound Treatment. International Journal of Antimicrobial Agents 2016, 48 (6), 732–735. https://doi.org/10.1016/j.ijantimicag.2016.08.014" in International Journal of Antimicrobial Agents (2016).

Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment

Spasojević, Dragica; Zmejkoski, Danica; Glamoclija, Jasmina; Nikolić, Miloš; Soković, Marina; Milošević, Verica; Jarić, Ivana; Stojanović, Marijana M.; Marinković, Emilija; Barisani-Asenbauer, Talin; Prodanović, Radivoje; Jovanović, Miloš; Radotić, Ksenija

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Zmejkoski, Danica
AU  - Glamoclija, Jasmina
AU  - Nikolić, Miloš
AU  - Soković, Marina
AU  - Milošević, Verica
AU  - Jarić, Ivana
AU  - Stojanović, Marijana M.
AU  - Marinković, Emilija
AU  - Barisani-Asenbauer, Talin
AU  - Prodanović, Radivoje
AU  - Jovanović, Miloš
AU  - Radotić, Ksenija
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2364
AB  - Nowadays bacterial resistance to known antibiotics is a serious health problem. In order to achieve more efficient treatment, lately there is an effort to find new substances, such as certain biomaterials, that are non-toxic to humans with antibiotic potential. Lignins and lignin-derived compounds have been proposed to be good candidates for use in medicine and health maintenance. In this study, the antibacterial activity of the lignin model polymer dehydrogenate polymer (DHP) in alginate hydrogel (Alg) was studied. The obtained results show that DHP-Alg has strong antimicrobial activity against several bacterial strains and biofilms and does not have a toxic effect on human epithelial cells. These results strongly suggest its application as a wound healing agent or as an adjunct substance for wound treatments. (C) 2016 Elsevier B.V. and International Society of Chemotherapy. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - International Journal of Antimicrobial Agents
T1  - Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment
VL  - 48
IS  - 6
SP  - 732
EP  - 735
DO  - 10.1016/j.ijantimicag.2016.08.014
UR  - Kon_3180
ER  - 
@article{
author = "Spasojević, Dragica and Zmejkoski, Danica and Glamoclija, Jasmina and Nikolić, Miloš and Soković, Marina and Milošević, Verica and Jarić, Ivana and Stojanović, Marijana M. and Marinković, Emilija and Barisani-Asenbauer, Talin and Prodanović, Radivoje and Jovanović, Miloš and Radotić, Ksenija",
year = "2016",
abstract = "Nowadays bacterial resistance to known antibiotics is a serious health problem. In order to achieve more efficient treatment, lately there is an effort to find new substances, such as certain biomaterials, that are non-toxic to humans with antibiotic potential. Lignins and lignin-derived compounds have been proposed to be good candidates for use in medicine and health maintenance. In this study, the antibacterial activity of the lignin model polymer dehydrogenate polymer (DHP) in alginate hydrogel (Alg) was studied. The obtained results show that DHP-Alg has strong antimicrobial activity against several bacterial strains and biofilms and does not have a toxic effect on human epithelial cells. These results strongly suggest its application as a wound healing agent or as an adjunct substance for wound treatments. (C) 2016 Elsevier B.V. and International Society of Chemotherapy. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "International Journal of Antimicrobial Agents",
title = "Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment",
volume = "48",
number = "6",
pages = "732-735",
doi = "10.1016/j.ijantimicag.2016.08.014",
url = "Kon_3180"
}
Spasojević, D., Zmejkoski, D., Glamoclija, J., Nikolić, M., Soković, M., Milošević, V., Jarić, I., Stojanović, M. M., Marinković, E., Barisani-Asenbauer, T., Prodanović, R., Jovanović, M.,& Radotić, K.. (2016). Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment. in International Journal of Antimicrobial Agents
Elsevier Science Bv, Amsterdam., 48(6), 732-735.
https://doi.org/10.1016/j.ijantimicag.2016.08.014
Kon_3180
Spasojević D, Zmejkoski D, Glamoclija J, Nikolić M, Soković M, Milošević V, Jarić I, Stojanović MM, Marinković E, Barisani-Asenbauer T, Prodanović R, Jovanović M, Radotić K. Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment. in International Journal of Antimicrobial Agents. 2016;48(6):732-735.
doi:10.1016/j.ijantimicag.2016.08.014
Kon_3180 .
Spasojević, Dragica, Zmejkoski, Danica, Glamoclija, Jasmina, Nikolić, Miloš, Soković, Marina, Milošević, Verica, Jarić, Ivana, Stojanović, Marijana M., Marinković, Emilija, Barisani-Asenbauer, Talin, Prodanović, Radivoje, Jovanović, Miloš, Radotić, Ksenija, "Lignin model compound in alginate hydrogel: a strong antimicrobial agent with high potential in wound treatment" in International Journal of Antimicrobial Agents, 48, no. 6 (2016):732-735,
https://doi.org/10.1016/j.ijantimicag.2016.08.014 .,
Kon_3180 .
24
19
19

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

Prodanović, Olivera; Spasojević, Dragica; Prokopijević, Miloš; Radotić, Ksenija; Marković, Nevena; Blažić, Marija; Prodanović, Radivoje

(Elsevier Science Bv, Amsterdam, 2015)

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  - http://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
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"
}
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..
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;..
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).

Tyramine modified alginates via periodate oxidation for peroxidase induced hydrogel formation and immobilization

Prodanović, Olivera; Spasojević, Dragica; Prokopijević, Miloš; Radotić, Ksenija; Marković, Nevena; Blažić, Marija; Prodanović, Radivoje

(Elsevier Science Bv, Amsterdam, 2015)

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  - http://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
UR  - Kon_2921
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",
url = "Kon_2921"
}
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
Kon_2921
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
Kon_2921 .
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 .,
Kon_2921 .
20
17
19

Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Stojanović, Željko; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2014)

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - http://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
UR  - Kon_2651
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",
url = "Kon_2651"
}
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
Kon_2651
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
Kon_2651 .
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 .,
Kon_2651 .
14
12
13

Immobilization of chemically modified horseradish peroxidase within activated alginate beads

Spasojević, Dragica; Prokopijević, Miloš; Prodanović, Olivera; Pirtea, Marilen Gabriel; Radotić, Ksenija; Prodanović, Radivoje

(Assoc Chemical Engineers Serbia, Belgrade, 2014)

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Pirtea, Marilen Gabriel
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2014
UR  - http://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
UR  - Kon_2653
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",
url = "Kon_2653"
}
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
Kon_2653
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
Kon_2653 .
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 .,
Kon_2653 .
6
6
7

Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers

Prodanović, Olivera; Prokopijević, Miloš; Spasojević, Dragica; Stojanović, Željko; Radotić, Ksenija; Knezevic-Jugovic, Zorica D.; Prodanović, Radivoje

(Humana Press Inc, Totowa, 2012)

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Knezevic-Jugovic, Zorica D.
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1552
AB  - A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.
PB  - Humana Press Inc, Totowa
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
VL  - 168
IS  - 5
SP  - 1288
EP  - 1301
DO  - 10.1007/s12010-012-9857-7
UR  - Kon_2383
ER  - 
@article{
author = "Prodanović, Olivera and Prokopijević, Miloš and Spasojević, Dragica and Stojanović, Željko and Radotić, Ksenija and Knezevic-Jugovic, Zorica D. and Prodanović, Radivoje",
year = "2012",
abstract = "A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.",
publisher = "Humana Press Inc, Totowa",
journal = "Applied Biochemistry and Biotechnology",
title = "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers",
volume = "168",
number = "5",
pages = "1288-1301",
doi = "10.1007/s12010-012-9857-7",
url = "Kon_2383"
}
Prodanović, O., Prokopijević, M., Spasojević, D., Stojanović, Ž., Radotić, K., Knezevic-Jugovic, Z. D.,& Prodanović, R.. (2012). Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology
Humana Press Inc, Totowa., 168(5), 1288-1301.
https://doi.org/10.1007/s12010-012-9857-7
Kon_2383
Prodanović O, Prokopijević M, Spasojević D, Stojanović Ž, Radotić K, Knezevic-Jugovic ZD, Prodanović R. Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology. 2012;168(5):1288-1301.
doi:10.1007/s12010-012-9857-7
Kon_2383 .
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