Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
Само за регистроване кориснике
2016
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.
Кључне речи:
Thermobifida fusca / Biocatalysis / Lignin / Peroxidase / Dye / VanillinИзвор:
Tetrahedron, 2016, 72, 46, 7276-7281Издавач:
- Pergamon-Elsevier Science Ltd, Oxford
Финансирање / пројекти:
DOI: 10.1016/j.tet.2015.12.078
ISSN: 0040-4020
WoS: 000386861000013
Scopus: 2-s2.0-84955263182
Институција/група
Inovacioni centar / Innovation CentreTY - JOUR AU - Lončar, Nikola L. AU - Colpa, Dana I. AU - Fraaije, Marco W. PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2342 AB - Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved. PB - Pergamon-Elsevier Science Ltd, Oxford T2 - Tetrahedron T1 - Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase VL - 72 IS - 46 SP - 7276 EP - 7281 DO - 10.1016/j.tet.2015.12.078 ER -
@article{ author = "Lončar, Nikola L. and Colpa, Dana I. and Fraaije, Marco W.", year = "2016", abstract = "Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.", publisher = "Pergamon-Elsevier Science Ltd, Oxford", journal = "Tetrahedron", title = "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase", volume = "72", number = "46", pages = "7276-7281", doi = "10.1016/j.tet.2015.12.078" }
Lončar, N. L., Colpa, D. I.,& Fraaije, M. W.. (2016). Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron Pergamon-Elsevier Science Ltd, Oxford., 72(46), 7276-7281. https://doi.org/10.1016/j.tet.2015.12.078
Lončar NL, Colpa DI, Fraaije MW. Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron. 2016;72(46):7276-7281. doi:10.1016/j.tet.2015.12.078 .
Lončar, Nikola L., Colpa, Dana I., Fraaije, Marco W., "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase" in Tetrahedron, 72, no. 46 (2016):7276-7281, https://doi.org/10.1016/j.tet.2015.12.078 . .