Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

Cristina M. Cordas, Giang Son Nguyen, Gabriel N. Valério, Malene Jønsson, Katharina Söllner, Ingvild H. Aune, Alexander Wentzel, José J. G. Moura

Research output: Contribution to journalArticlepeer-review

Abstract

A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry.

Original languageEnglish
Article number111651
JournalJournal of Inorganic Biochemistry
Volume226
DOIs
Publication statusPublished - Jan 2022

Keywords

  • Actinobacteria
  • Catalysis
  • Data mining
  • Dye-decolorizing peroxidase
  • Electrochemistry
  • Profile hidden Markov model

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