Two-way reaction of versatile peroxidase with artificial lignin enhances low-molecular weight fractions
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2023
Authors
Spasojević, DragicaProdanović, Olivera
Mutavdžić, Dragosav
Šekuljica, Nataša
Jovanović, Jelena
Maksimović, Vuk
Radotić, Ksenija
Article (Published version)
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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 w...ell 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.
Keywords:
artificial lignin / oligomer fractions / PCA / RP-HPLC-MS / ultrafiltration / versatile peroxidaseSource:
Biotechnology Journal, 2023Publisher:
- John Wiley and Sons Inc
Funding / projects:
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200053 (University of Belgrade, Institute for Multidisciplinary Research) (RS-MESTD-inst-2020-200053)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200135 (University of Belgrade, Faculty of Technology and Metallurgy) (RS-MESTD-inst-2020-200135)
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200287 (Innovation Center of the Faculty of Technology and Metallurgy) (RS-MESTD-inst-2020-200287)
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Inovacioni centarTY - 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 . .