Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
| Autor: | Nikola Lončar, Marco W. Fraaije, Dana I. Colpa |
|---|---|
| Přispěvatelé: | Biotechnology |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
DECOLORIZING PEROXIDASE Dye DIVANILLIN 030106 microbiology RHODOCOCCUS-JOSTII RHA1 ALCOHOL OXIDATION Biochemistry Horseradish peroxidase Lignin 03 medical and health sciences chemistry.chemical_compound Thermobifida fusca Drug Discovery Oxidative enzyme Peroxidase biology IDENTIFICATION Organic Chemistry HORSERADISH-PEROXIDASE FAMILY 030104 developmental biology chemistry Biocatalysis Vanillin biology.protein DYES |
| Zdroj: | Tetrahedron, 72(46), 7276-7281. PERGAMON-ELSEVIER SCIENCE LTD Tetrahedron |
| ISSN: | 1464-5416 0040-4020 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect