Efficient Oxidation of 5-Hydroxymethylfurfural Using a Flavoprotein Oxidase from the Honeybee Apis mellifera

Gwen Tjallinks*, Alessandro Boverio, Amarins W Jager, Saniye G Kaya, Andrea Mattevi, Marco W Fraaije*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
64 Downloads (Pure)

Abstract

The chemical 5-hydroxymethyl-furfural (HMF) can be derived from lignocellulose and is an interesting bio-based platform chemical as it has the potential to be transformed into numerous valuable building blocks such as the polymer-precursor 2,5-diformylfuran (DFF). To date, only few oxidases acting on HMF are known and by sampling atypical species, we discovered a novel flavin-dependent oxidoreductase from the honeybee Apis mellifera (beeHMFO). The enzyme can perform the chemo-selective oxidation of HMF to DFF but can also readily accept other aromatic alcohols as substrates. The function of the enzyme may well be the antimicrobial generation of hydrogen peroxide using HMF, which is very abundant in honey. The discovery of this insect-derived flavoprotein oxidase holds promising potential in the synthesis of renewable products and demonstrates that insects can be an interesting source for novel biocatalysts.

Original languageEnglish
Article numbere202300588
Number of pages7
JournalChemBioChem
Volume24
Issue number24
Early online date6-Oct-2023
DOIs
Publication statusPublished - 14-Dec-2023

Keywords

  • 5-hydroxymethylfurfural
  • Apis mellifera
  • biocatalysis
  • flavoprotein
  • oxidoreductase

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