Exploring the biochemical and biocatalytic properties of bacterial DyP-type peroxidases

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This thesis describes the research on two dye decolorizing peroxidases (DyP-type peroxidases). As the name of this enzyme family suggests, are these enzyme involved in the decolorization and degradation of in water soluble dyes. The textile and food industries are potential application fields of this enzyme family.
The main goal of the research described in this thesis was to increase the knowledge on DyP-type peroxidases. Two bacterial enzymes were selected as model enzymes: TfuDyP from Thermobifida fusca and SviDyP from Saccharomonospora viridis. First, we studied on which compounds TfuDyP is active. This work showed that the enzyme is, among other compounds, active on phenols and a large variety of dyes, including dyes that were not studied before using DyP-type peroxidases (chapter 2). Furthermore, the reaction mechanism of the enzyme was studied (chapter 3). For the industrial applicability of enzymes an easy production method with a high enzyme yield is required. Chapter 4 describes a study aimed at optimizing the production of active TfuDyP. To be active, DyP-type peroxidases need to bind a heme cofactor. Results presented in chapter 4 provide crucial information on what can go wrong with the heme cofactor when a heme-containing protein is overexpressed (produced). Finally we fused SviDyP to four different oxidases (another type of enzyme) to perform two-step cascade reactions (chapter 5). With these fusion enzymes we were able to produce the taste enhancer divanilline and to detect the sugars xylitol and cellobiose in a solution.
Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • University of Groningen
  • Fraaije, Marco, Supervisor
  • Janssen, Dick, Assessment committee
  • Maglia, Giovanni, Assessment committee
  • Martins, L., Assessment committee, External person
Award date26-Oct-2018
Place of Publication[Groningen]
Print ISBNs978-94-034-1070-8
Electronic ISBNs978-94-034-1069-2
Publication statusPublished - 2018

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