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  - 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 . .