TY  - DATA
AU  - Stanković, Mira
AU  - Prokopijević, Miloš
AU  - Šikoparija, Branko
AU  - Nedić, Nebojša
AU  - Andrić, Filip
AU  - Polović, Natalija
AU  - Natić, Maja
AU  - Radotić, Ksenija
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5848
AB  - Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We examined whether the parameters of the honey samples’ fluorescence spectra and biochemical parameters, both related to proteins and phenolics, may be connected with the level of honey bee colonies’ infestation. The infestation level was highly positively correlated with the catalase activity in honey (r = 0.936). Additionally, the infestation level was positively correlated with the phenolic spectral component (r = 0.656), which was tentatively related to the phenolics in honey. No correlation was found between the diastase activity in honey and the colonies’ infestation level. The results indicate that the catalase activity in honey and the PFC1 spectral component may be reliable markers for the V. destructor infestation level of the colonies. The obtained data may be related to the honey yield obtained from the apiaries.
T2  - Foods
T2  - Foods
T1  - Supplementary material for: Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629
VL  - 12
IS  - 3
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5848
ER  - 

@misc{
author = "Stanković, Mira and Prokopijević, Miloš and Šikoparija, Branko and Nedić, Nebojša and Andrić, Filip and Polović, Natalija and Natić, Maja and Radotić, Ksenija",
year = "2023",
abstract = "Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We examined whether the parameters of the honey samples’ fluorescence spectra and biochemical parameters, both related to proteins and phenolics, may be connected with the level of honey bee colonies’ infestation. The infestation level was highly positively correlated with the catalase activity in honey (r = 0.936). Additionally, the infestation level was positively correlated with the phenolic spectral component (r = 0.656), which was tentatively related to the phenolics in honey. No correlation was found between the diastase activity in honey and the colonies’ infestation level. The results indicate that the catalase activity in honey and the PFC1 spectral component may be reliable markers for the V. destructor infestation level of the colonies. The obtained data may be related to the honey yield obtained from the apiaries.",
journal = "Foods, Foods",
title = "Supplementary material for: Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629",
volume = "12",
number = "3",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5848"
}

Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Supplementary material for: Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629. in Foods, 12(3).
https://hdl.handle.net/21.15107/rcub_cherry_5848

Stanković M, Prokopijević M, Šikoparija B, Nedić N, Andrić F, Polović N, Natić M, Radotić K. Supplementary material for: Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629. in Foods. 2023;12(3).
https://hdl.handle.net/21.15107/rcub_cherry_5848 .

Stanković, Mira, Prokopijević, Miloš, Šikoparija, Branko, Nedić, Nebojša, Andrić, Filip, Polović, Natalija, Natić, Maja, Radotić, Ksenija, "Supplementary material for: Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629" in Foods, 12, no. 3 (2023),
https://hdl.handle.net/21.15107/rcub_cherry_5848 .

TY  - JOUR
AU  - Stanković, Mira
AU  - Prokopijević, Miloš
AU  - Šikoparija, Branko
AU  - Nedić, Nebojša
AU  - Andrić, Filip
AU  - Polović, Natalija
AU  - Natić, Maja
AU  - Radotić, Ksenija
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5847
AB  - Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We examined whether the parameters of the honey samples’ fluorescence spectra and biochemical parameters, both related to proteins and phenolics, may be connected with the level of honey bee colonies’ infestation. The infestation level was highly positively correlated with the catalase activity in honey (r = 0.936). Additionally, the infestation level was positively correlated with the phenolic spectral component (r = 0.656), which was tentatively related to the phenolics in honey. No correlation was found between the diastase activity in honey and the colonies’ infestation level. The results indicate that the catalase activity in honey and the PFC1 spectral component may be reliable markers for the V. destructor infestation level of the colonies. The obtained data may be related to the honey yield obtained from the apiaries.
T2  - Foods
T2  - Foods
T1  - Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies
VL  - 12
IS  - 3
SP  - 629
DO  - 10.3390/foods12030629
ER  - 

@article{
author = "Stanković, Mira and Prokopijević, Miloš and Šikoparija, Branko and Nedić, Nebojša and Andrić, Filip and Polović, Natalija and Natić, Maja and Radotić, Ksenija",
year = "2023",
abstract = "Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We examined whether the parameters of the honey samples’ fluorescence spectra and biochemical parameters, both related to proteins and phenolics, may be connected with the level of honey bee colonies’ infestation. The infestation level was highly positively correlated with the catalase activity in honey (r = 0.936). Additionally, the infestation level was positively correlated with the phenolic spectral component (r = 0.656), which was tentatively related to the phenolics in honey. No correlation was found between the diastase activity in honey and the colonies’ infestation level. The results indicate that the catalase activity in honey and the PFC1 spectral component may be reliable markers for the V. destructor infestation level of the colonies. The obtained data may be related to the honey yield obtained from the apiaries.",
journal = "Foods, Foods",
title = "Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies",
volume = "12",
number = "3",
pages = "629",
doi = "10.3390/foods12030629"
}

Stanković, M., Prokopijević, M., Šikoparija, B., Nedić, N., Andrić, F., Polović, N., Natić, M.,& Radotić, K.. (2023). Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods, 12(3), 629.
https://doi.org/10.3390/foods12030629

Stanković M, Prokopijević M, Šikoparija B, Nedić N, Andrić F, Polović N, Natić M, Radotić K. Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies. in Foods. 2023;12(3):629.
doi:10.3390/foods12030629 .

Stanković, Mira, Prokopijević, Miloš, Šikoparija, Branko, Nedić, Nebojša, Andrić, Filip, Polović, Natalija, Natić, Maja, Radotić, Ksenija, "Using Front-Face Fluorescence Spectroscopy and Biochemical
Analysis of Honey to Assess a Marker for the Level of Varroa
destructor Infestation of Honey Bee (Apis mellifera) Colonies" in Foods, 12, no. 3 (2023):629,
https://doi.org/10.3390/foods12030629 . .

TY  - JOUR
AU  - Bartolić, Dragana
AU  - Mojović, Miloš
AU  - Prokopijević, Miloš
AU  - Đikanović, Daniela
AU  - Kalauzi, Aleksandar
AU  - Mutavdžić, Dragosav
AU  - Baošić, Rada
AU  - Radotić, Ksenija
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5268
AB  - Aflatoxin B1 (AFB1), is a naturally hazardous environmental contaminant, contained mainly in various cereal seeds. The maize (Zea mays L.) seeds containing various levels of the AFB1 was investigated using optical and electron paramagnetic resonance spectroscopies. The changes of lignin content and organic free radicals as indicators of the seeds' defense response to the AFB1-stressor were estimated, in the seeds' inner and outer fractions. The lignin content was determined using the Acetyl Bromide method. No correlation was found between the lignin content and the AFB1 concentration in the inner fraction (R of 0.030, p = 0.943), while a significant positive linear correlation (R of 0.9923, p= 0.00005) between the lignin content and the AFB1 concentration in the outer fraction was obtained. Employing electron paramagnetic resonance (EPR) spectroscopy, the different response of the fractions was observed, regarding the content of free radicals with increasing AFB1 concentrations. In addition, front-face fluorescence spectroscopy in combination with the deconvolution showed a positive linear correlation between the ratio of the green and blue spectral emission components (C4/C2) area and the AFB1 concentration in the outer fraction. Thus lignin content and the (C4/C2) area ratio may be reliable indicators for the screening of lignin changes related to the level of AFB1 in the seeds.
PB  - Wiley
T2  - Journal of the Science of Food and Agriculture
T1  - Lignin and organic free radicals in maize (Zea mays  L.) seeds in response to aflatoxin B1 contamination: an optical and EPR spectroscopic study
VL  - 102
IS  - 6
SP  - 2500
EP  - 2505
DO  - 10.1002/jsfa.11591
ER  - 

@article{
author = "Bartolić, Dragana and Mojović, Miloš and Prokopijević, Miloš and Đikanović, Daniela and Kalauzi, Aleksandar and Mutavdžić, Dragosav and Baošić, Rada and Radotić, Ksenija",
year = "2022",
abstract = "Aflatoxin B1 (AFB1), is a naturally hazardous environmental contaminant, contained mainly in various cereal seeds. The maize (Zea mays L.) seeds containing various levels of the AFB1 was investigated using optical and electron paramagnetic resonance spectroscopies. The changes of lignin content and organic free radicals as indicators of the seeds' defense response to the AFB1-stressor were estimated, in the seeds' inner and outer fractions. The lignin content was determined using the Acetyl Bromide method. No correlation was found between the lignin content and the AFB1 concentration in the inner fraction (R of 0.030, p = 0.943), while a significant positive linear correlation (R of 0.9923, p= 0.00005) between the lignin content and the AFB1 concentration in the outer fraction was obtained. Employing electron paramagnetic resonance (EPR) spectroscopy, the different response of the fractions was observed, regarding the content of free radicals with increasing AFB1 concentrations. In addition, front-face fluorescence spectroscopy in combination with the deconvolution showed a positive linear correlation between the ratio of the green and blue spectral emission components (C4/C2) area and the AFB1 concentration in the outer fraction. Thus lignin content and the (C4/C2) area ratio may be reliable indicators for the screening of lignin changes related to the level of AFB1 in the seeds.",
publisher = "Wiley",
journal = "Journal of the Science of Food and Agriculture",
title = "Lignin and organic free radicals in maize (Zea mays  L.) seeds in response to aflatoxin B1 contamination: an optical and EPR spectroscopic study",
volume = "102",
number = "6",
pages = "2500-2505",
doi = "10.1002/jsfa.11591"
}

Bartolić, D., Mojović, M., Prokopijević, M., Đikanović, D., Kalauzi, A., Mutavdžić, D., Baošić, R.,& Radotić, K.. (2022). Lignin and organic free radicals in maize (Zea mays  L.) seeds in response to aflatoxin B1 contamination: an optical and EPR spectroscopic study. in Journal of the Science of Food and Agriculture
Wiley., 102(6), 2500-2505.
https://doi.org/10.1002/jsfa.11591

Bartolić D, Mojović M, Prokopijević M, Đikanović D, Kalauzi A, Mutavdžić D, Baošić R, Radotić K. Lignin and organic free radicals in maize (Zea mays  L.) seeds in response to aflatoxin B1 contamination: an optical and EPR spectroscopic study. in Journal of the Science of Food and Agriculture. 2022;102(6):2500-2505.
doi:10.1002/jsfa.11591 .

Bartolić, Dragana, Mojović, Miloš, Prokopijević, Miloš, Đikanović, Daniela, Kalauzi, Aleksandar, Mutavdžić, Dragosav, Baošić, Rada, Radotić, Ksenija, "Lignin and organic free radicals in maize (Zea mays  L.) seeds in response to aflatoxin B1 contamination: an optical and EPR spectroscopic study" in Journal of the Science of Food and Agriculture, 102, no. 6 (2022):2500-2505,
https://doi.org/10.1002/jsfa.11591 . .

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  - 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  - THES
AU  - Prokopijević, Miloš
PY  - 2017
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=5591
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:17096/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=49839119
UR  - http://nardus.mpn.gov.rs/123456789/9174
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2745
AB  - Peroksidaza iz soje (SBP, E.C. 1.11.1.7) je enzim koji pripada klasi III biljnih peroksidaza i katalizuje oksidaciju i polimerizaciju različitih fenolnih jedinjenja u prisustvu vodonik peroksida kao supstrata. Nalazi se u semenom omotaču soje koji predstavlja jeftini nusproizvod i polazni materijal za izolovanje velike količine sirovog enzima.Izolovana SBP je imobilizovana primenom dve kovalentne metode na seriju makroporoznih kopolimera poli(GMA-co-EGDMA) različitih dijametara pora. Glutaraldehidni metod imobilizacije se pokazao boljim od perjodatnog a najveća specifična aktivnost od 23 IU/g dobijena je na kopolimeru veličine pora od 120 nm. Imobilizovana peroksidaza pokazala je veću termalnu stabilnost i stabilnost u organskom rastvaraču, aktivnost u širem opsegu pH i 2,86 puta veću Km vrednost za pirogalol u odnosu na rastvorni enzim.Sintetisana je serija modifikovanih pektina oksidacijom perjodatom u molarnom odnosu od 2,5 do 20 mol% i naknadnom reduktivnom aminacijom tiraminom i cijanoborhidridom. Dobijeni tiramin-pektini prave stabilne hidrogelove umrežavanjem fenolnih grupa u reakciji katalizovanoj peroksidazama u prisustvu vodonik peroksida. SBP je uspešno imobilizovana unutar mikro-kuglica hidrogela nastalih enzimskom polimerizacijom modifikovanog pektina u emulziji sa najvećom specifičnom aktivnošću postignutom na tiramin-pektinu oksidovanom 5 mol% perjodatom. Imobilizovana SBP je pored šireg pH optimuma pokazala i veću termalnu stabilnost i stabilnost u organskom rastvaraču u odnosu na slobodan enzim. Mikrokuglice sa imobilizovanom SBP zadržale su 50% početne aktivnosti nakon 7 ciklusa ponovne upotrebe za oksidaciju pirogalola u bač reaktoru.Pod optimalnim uslovima sa unutrašnjom dostavom vodonik peroksida postignuto je uklanjanje fenola od 64% imobilizovanom SBP na poli(GMA-co-EGDMA) veličine pora od 120 nm.
AB  - Soybean peroxidase (SBP, E.C. 1.11.1.7) is an enzyme that belongs to class III of plant peroxidases that catalyses oxidation and polymerization of various phenolic compounds in the presence of hydrogen peroxide as substrate. It's located in the soybean seed hulls, an inexpensive byproduct and excellent material for isolation of large amounts of crude enzyme.SBP was immobilized by using two covalent methods onto a series of macroporous copolymers of poly(GMA-co-EGDMA) with various pore diameters. Glutaraldehyde immobilization method proved to be better than periodate with highest specific activity of 23 IU/g obtained with copolymer with pore size of 120 nm. Compared to the soluble enzyme, immobilized peroxidase showed increased thermal and organic solvent stability, broader pH activity range and 2.86 times higher Km value for pyrogallol.Series of modified pectins have been synthesized by oxidation with periodate in molar ratios from 2.5 to 20 mol% and subsequent reductive amination with tyramine and cyanobohrhydride. Obtained tyramnine-pectine made stable hydrogels by crosslinking phenol groups in a peroxidase catalysed reaction in the presence of hydrogen peroxide. SBP was immobilized within hydrogel microbeads created in enzyme polymerization of modified pectin in emulsion with highest specific activity achieved with tyramine-pectin oxidized by 5 mol% of periodate. Immobilized SBP in addition of having wider pH optimum showed higher thermal and organic solvent stability compared to the free enzyme. SBP bound in microbeads retained 50% of the original activity after 7 cycles of repeated usage for pyrogallol oxidation in batch reactor.Under optimal conditions with internal hydrogen peroxide delivery phenol removal of 64% has been achieved with SBP immobilized onto poly(GMA-co-EGDMA) with pore size of 120 nm.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Imobilizacija peroksidaze iz soje (Glycine max) na makroporoznom glicidil-metakrilatu i hemijski modifikovanom pektinu
UR  - https://hdl.handle.net/21.15107/rcub_nardus_9174
ER  - 

@phdthesis{
author = "Prokopijević, Miloš",
year = "2017",
abstract = "Peroksidaza iz soje (SBP, E.C. 1.11.1.7) je enzim koji pripada klasi III biljnih peroksidaza i katalizuje oksidaciju i polimerizaciju različitih fenolnih jedinjenja u prisustvu vodonik peroksida kao supstrata. Nalazi se u semenom omotaču soje koji predstavlja jeftini nusproizvod i polazni materijal za izolovanje velike količine sirovog enzima.Izolovana SBP je imobilizovana primenom dve kovalentne metode na seriju makroporoznih kopolimera poli(GMA-co-EGDMA) različitih dijametara pora. Glutaraldehidni metod imobilizacije se pokazao boljim od perjodatnog a najveća specifična aktivnost od 23 IU/g dobijena je na kopolimeru veličine pora od 120 nm. Imobilizovana peroksidaza pokazala je veću termalnu stabilnost i stabilnost u organskom rastvaraču, aktivnost u širem opsegu pH i 2,86 puta veću Km vrednost za pirogalol u odnosu na rastvorni enzim.Sintetisana je serija modifikovanih pektina oksidacijom perjodatom u molarnom odnosu od 2,5 do 20 mol% i naknadnom reduktivnom aminacijom tiraminom i cijanoborhidridom. Dobijeni tiramin-pektini prave stabilne hidrogelove umrežavanjem fenolnih grupa u reakciji katalizovanoj peroksidazama u prisustvu vodonik peroksida. SBP je uspešno imobilizovana unutar mikro-kuglica hidrogela nastalih enzimskom polimerizacijom modifikovanog pektina u emulziji sa najvećom specifičnom aktivnošću postignutom na tiramin-pektinu oksidovanom 5 mol% perjodatom. Imobilizovana SBP je pored šireg pH optimuma pokazala i veću termalnu stabilnost i stabilnost u organskom rastvaraču u odnosu na slobodan enzim. Mikrokuglice sa imobilizovanom SBP zadržale su 50% početne aktivnosti nakon 7 ciklusa ponovne upotrebe za oksidaciju pirogalola u bač reaktoru.Pod optimalnim uslovima sa unutrašnjom dostavom vodonik peroksida postignuto je uklanjanje fenola od 64% imobilizovanom SBP na poli(GMA-co-EGDMA) veličine pora od 120 nm., Soybean peroxidase (SBP, E.C. 1.11.1.7) is an enzyme that belongs to class III of plant peroxidases that catalyses oxidation and polymerization of various phenolic compounds in the presence of hydrogen peroxide as substrate. It's located in the soybean seed hulls, an inexpensive byproduct and excellent material for isolation of large amounts of crude enzyme.SBP was immobilized by using two covalent methods onto a series of macroporous copolymers of poly(GMA-co-EGDMA) with various pore diameters. Glutaraldehyde immobilization method proved to be better than periodate with highest specific activity of 23 IU/g obtained with copolymer with pore size of 120 nm. Compared to the soluble enzyme, immobilized peroxidase showed increased thermal and organic solvent stability, broader pH activity range and 2.86 times higher Km value for pyrogallol.Series of modified pectins have been synthesized by oxidation with periodate in molar ratios from 2.5 to 20 mol% and subsequent reductive amination with tyramine and cyanobohrhydride. Obtained tyramnine-pectine made stable hydrogels by crosslinking phenol groups in a peroxidase catalysed reaction in the presence of hydrogen peroxide. SBP was immobilized within hydrogel microbeads created in enzyme polymerization of modified pectin in emulsion with highest specific activity achieved with tyramine-pectin oxidized by 5 mol% of periodate. Immobilized SBP in addition of having wider pH optimum showed higher thermal and organic solvent stability compared to the free enzyme. SBP bound in microbeads retained 50% of the original activity after 7 cycles of repeated usage for pyrogallol oxidation in batch reactor.Under optimal conditions with internal hydrogen peroxide delivery phenol removal of 64% has been achieved with SBP immobilized onto poly(GMA-co-EGDMA) with pore size of 120 nm.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Imobilizacija peroksidaze iz soje (Glycine max) na makroporoznom glicidil-metakrilatu i hemijski modifikovanom pektinu",
url = "https://hdl.handle.net/21.15107/rcub_nardus_9174"
}

Prokopijević, M.. (2017). Imobilizacija peroksidaze iz soje (Glycine max) na makroporoznom glicidil-metakrilatu i hemijski modifikovanom pektinu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_9174

Prokopijević M. Imobilizacija peroksidaze iz soje (Glycine max) na makroporoznom glicidil-metakrilatu i hemijski modifikovanom pektinu. in Универзитет у Београду. 2017;.
https://hdl.handle.net/21.15107/rcub_nardus_9174 .

Prokopijević, Miloš, "Imobilizacija peroksidaze iz soje (Glycine max) na makroporoznom glicidil-metakrilatu i hemijski modifikovanom pektinu" in Универзитет у Београду (2017),
https://hdl.handle.net/21.15107/rcub_nardus_9174 .

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  - 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  - https://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
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"
}

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

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 .

Prodanović, Olivera, Prokopijević, Miloš, Spasojević, Dragica, Stojanović, Željko, Radotić, Ksenija, Knezevic-Jugovic, Zorica D., Prodanović, Radivoje, "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers" in Applied Biochemistry and Biotechnology, 168, no. 5 (2012):1288-1301,
https://doi.org/10.1007/s12010-012-9857-7 . .