TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prodanović, Olivera
AU  - Mutavdžić, Dragosav
AU  - Šekuljica, Nataša
AU  - Jovanović, Jelena
AU  - Maksimović, Vuk
AU  - Radotić, Ksenija
PY  - 2023
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6635
AB  - In recent years, versatile peroxidase (VP) has emerged as a promising enzyme for biotechnological applications, as it can oxidize lignin without the external mediators. To gain insights into the breakdown process of artificial lignin by VP, reaction between the two was studied. Degradation products were fractionated using ultrafiltration and analyzed by RP- high performance liquid chromatography with mass detection (HPLC-MS) chromatography. Four fractions were obtained based on their molecular sizes: >10, 3–10, 1–3, and <1 kDa. Interestingly, while VP did not significantly alter the yields of these fractions, the chromatograms revealed the presence of oligomers with different molecular weights (MWs) resulting from the enzymatic activity. The VP exhibits a dual role in its enzymatic activity: both degrading and synthesizing these oligomers. This was confirmed by principal component analysis (PCA). The positive correlations were found between certain oligomers (D1 and D2, D5 and D6, as well as between D7, D10, T2, and T4), suggesting their simultaneous degradation. On the other hand, a negative correlation was found between the monomer and some oligomers (D7, D10, T2, and T4), indicating the decomposition of these oligomers into monomers. These findings shed light on the intricate interplay between VP and artificial lignin, offering valuable insights for potential applications in lignin valorization.
PB  - John Wiley and Sons Inc
T2  - Biotechnology Journal
T1  - Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions
DO  - 10.1002/biot.202300312
ER  - 

@article{
author = "Spasojević, Dragica and Prodanović, Olivera and Mutavdžić, Dragosav and Šekuljica, Nataša and Jovanović, Jelena and Maksimović, Vuk and Radotić, Ksenija",
year = "2023",
abstract = "In recent years, versatile peroxidase (VP) has emerged as a promising enzyme for biotechnological applications, as it can oxidize lignin without the external mediators. To gain insights into the breakdown process of artificial lignin by VP, reaction between the two was studied. Degradation products were fractionated using ultrafiltration and analyzed by RP- high performance liquid chromatography with mass detection (HPLC-MS) chromatography. Four fractions were obtained based on their molecular sizes: >10, 3–10, 1–3, and <1 kDa. Interestingly, while VP did not significantly alter the yields of these fractions, the chromatograms revealed the presence of oligomers with different molecular weights (MWs) resulting from the enzymatic activity. The VP exhibits a dual role in its enzymatic activity: both degrading and synthesizing these oligomers. This was confirmed by principal component analysis (PCA). The positive correlations were found between certain oligomers (D1 and D2, D5 and D6, as well as between D7, D10, T2, and T4), suggesting their simultaneous degradation. On the other hand, a negative correlation was found between the monomer and some oligomers (D7, D10, T2, and T4), indicating the decomposition of these oligomers into monomers. These findings shed light on the intricate interplay between VP and artificial lignin, offering valuable insights for potential applications in lignin valorization.",
publisher = "John Wiley and Sons Inc",
journal = "Biotechnology Journal",
title = "Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions",
doi = "10.1002/biot.202300312"
}

Spasojević, D., Prodanović, O., Mutavdžić, D., Šekuljica, N., Jovanović, J., Maksimović, V.,& Radotić, K.. (2023). Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions. in Biotechnology Journal
John Wiley and Sons Inc..
https://doi.org/10.1002/biot.202300312

Spasojević D, Prodanović O, Mutavdžić D, Šekuljica N, Jovanović J, Maksimović V, Radotić K. Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions. in Biotechnology Journal. 2023;.
doi:10.1002/biot.202300312 .

Spasojević, Dragica, Prodanović, Olivera, Mutavdžić, Dragosav, Šekuljica, Nataša, Jovanović, Jelena, Maksimović, Vuk, Radotić, Ksenija, "Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions" in Biotechnology Journal (2023),
https://doi.org/10.1002/biot.202300312 . .

TY  - JOUR
AU  - Pantić, Nevena
AU  - Spasojević, Milica
AU  - Stojanović, Željko
AU  - Veljović, Đorđe
AU  - Krstić, Jugoslav
AU  - Balaž, Ana Marija
AU  - Prodanović, Radivoje
AU  - Prodanović, Olivera
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5096
AB  - Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.
PB  - Springer
T2  - Journal of Polymers and the Environment
T1  - Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol
DO  - 10.1007/s10924-021-02364-3
ER  - 

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

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

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

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

TY  - JOUR
AU  - Moftah, Omar A.S.
AU  - Grbavčić, Sanja
AU  - Moftah, Walid A.S.
AU  - Luković, Nevena
AU  - Prodanović, Olivera
AU  - Jakovetić, Sonja
AU  - Knežević-Jugović, Zorica
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2362
AB  - In this study, the solid and liquid wastes from the olive oil processing industry were evaluated as substrates for Yarrowia lipolytica growth with the aim of lipase production. Olive mill wastewater and olive oil cake seemed to provide the necessary nutrients and physical support for yeast growth and enzyme production. The highest lipolytic activity of 850 IU dm-3 was achieved after 4 days of submerged cultivation in supplemented olive mill wastewater. In addition, olive oil cake appeared to be a convenient substrate for lipase production under a solid-state fermentation mode. Lipase production was further improved by media supplementation and/or change in the physical settings of the experiment. However, the most significant improvement of lipase production under solid-state fermentation was achieved by an alkaline treatment of the substrate (more than 10-fold), when the amount of produced lipase reached up to ≈40 IU g-1 of substrate.
AB  - U ovom radu, tečne i čvrste otpadne sirovine koje zaostaju prilikom prerade maslina ispitane su kao potencijalni supstrati za rast kvasca Yarrowia lipolytica sa ciljem proizvodnje lipaza. Otpadna voda iz mlina, kao i pogača koja zaostaje nakon ceđenja ulja iz maslina, pokazali su se kao dobri izvori nutrijenata za rast ovog kvasca i proizvodnju enzima. U optimizovanoj tečnoj podlozi, prinos lipaza dostiže i do 850 IU dm-3. Pored toga, pogača koja zaostaje nakon ceđenja ulja iz maslina se pokazala kao pogodan čvrsti supstrat za gajenje proizvodnog mikroorganizma. Produkcija lipaza na ovom medijumu je dodatno optimizovana suplementacijom različitim izvorima azota i ugljenika, kao i promenom ostalih parametara fermentacije. Utvrđeno je da se najznačajnije poboljšanje produkcije lipaze ostvaruje alkalnim predtretmanom supstrata (više od 10 puta).
PB  - Serbian Chemical Society, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates
T1  - Proizvodnja lipaze iz Yarrowia lipolytica korišćenjem otpadnih sirovina industrije prerade maslina kao supstrata
EP  - 794
IS  - 6
SP  - 781
VL  - 78
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2362
ER  - 

@article{
author = "Moftah, Omar A.S. and Grbavčić, Sanja and Moftah, Walid A.S. and Luković, Nevena and Prodanović, Olivera and Jakovetić, Sonja and Knežević-Jugović, Zorica",
year = "2013",
abstract = "In this study, the solid and liquid wastes from the olive oil processing industry were evaluated as substrates for Yarrowia lipolytica growth with the aim of lipase production. Olive mill wastewater and olive oil cake seemed to provide the necessary nutrients and physical support for yeast growth and enzyme production. The highest lipolytic activity of 850 IU dm-3 was achieved after 4 days of submerged cultivation in supplemented olive mill wastewater. In addition, olive oil cake appeared to be a convenient substrate for lipase production under a solid-state fermentation mode. Lipase production was further improved by media supplementation and/or change in the physical settings of the experiment. However, the most significant improvement of lipase production under solid-state fermentation was achieved by an alkaline treatment of the substrate (more than 10-fold), when the amount of produced lipase reached up to ≈40 IU g-1 of substrate., U ovom radu, tečne i čvrste otpadne sirovine koje zaostaju prilikom prerade maslina ispitane su kao potencijalni supstrati za rast kvasca Yarrowia lipolytica sa ciljem proizvodnje lipaza. Otpadna voda iz mlina, kao i pogača koja zaostaje nakon ceđenja ulja iz maslina, pokazali su se kao dobri izvori nutrijenata za rast ovog kvasca i proizvodnju enzima. U optimizovanoj tečnoj podlozi, prinos lipaza dostiže i do 850 IU dm-3. Pored toga, pogača koja zaostaje nakon ceđenja ulja iz maslina se pokazala kao pogodan čvrsti supstrat za gajenje proizvodnog mikroorganizma. Produkcija lipaza na ovom medijumu je dodatno optimizovana suplementacijom različitim izvorima azota i ugljenika, kao i promenom ostalih parametara fermentacije. Utvrđeno je da se najznačajnije poboljšanje produkcije lipaze ostvaruje alkalnim predtretmanom supstrata (više od 10 puta).",
publisher = "Serbian Chemical Society, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates, Proizvodnja lipaze iz Yarrowia lipolytica korišćenjem otpadnih sirovina industrije prerade maslina kao supstrata",
pages = "794-781",
number = "6",
volume = "78",
url = "https://hdl.handle.net/21.15107/rcub_technorep_2362"
}

Moftah, O. A.S., Grbavčić, S., Moftah, W. A.S., Luković, N., Prodanović, O., Jakovetić, S.,& Knežević-Jugović, Z.. (2013). Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates. in Journal of the Serbian Chemical Society
Serbian Chemical Society, Belgrade., 78(6), 781-794.
https://hdl.handle.net/21.15107/rcub_technorep_2362

Moftah OA, Grbavčić S, Moftah WA, Luković N, Prodanović O, Jakovetić S, Knežević-Jugović Z. Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates. in Journal of the Serbian Chemical Society. 2013;78(6):781-794.
https://hdl.handle.net/21.15107/rcub_technorep_2362 .

Moftah, Omar A.S., Grbavčić, Sanja, Moftah, Walid A.S., Luković, Nevena, Prodanović, Olivera, Jakovetić, Sonja, Knežević-Jugović, Zorica, "Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates" in Journal of the Serbian Chemical Society, 78, no. 6 (2013):781-794,
https://hdl.handle.net/21.15107/rcub_technorep_2362 .

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Željko
AU  - Radotić, Ksenija
AU  - Knežević-Jugović, Zorica
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2187
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  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
EP  - 1301
IS  - 5
SP  - 1288
VL  - 168
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 Knežević-Jugović, Zorica 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 = "Springer, New York",
journal = "Applied Biochemistry and Biotechnology",
title = "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers",
pages = "1301-1288",
number = "5",
volume = "168",
doi = "10.1007/s12010-012-9857-7"
}

Prodanović, O., Prokopijević, M., Spasojević, D., Stojanović, Ž., Radotić, K., Knežević-Jugović, Z.,& Prodanović, R.. (2012). Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology
Springer, New York., 168(5), 1288-1301.
https://doi.org/10.1007/s12010-012-9857-7

Prodanović O, Prokopijević M, Spasojević D, Stojanović Ž, Radotić K, Knežević-Jugović Z, 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, Knežević-Jugović, Zorica, 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 . .