Your browser doesn't support javascript.
loading
Efficient Oxidation of 5-Hydroxymethylfurfural Using a Flavoprotein Oxidase from the Honeybee Apis mellifera.
Tjallinks, Gwen; Boverio, Alessandro; Jager, Amarins W; Kaya, Saniye G; Mattevi, Andrea; Fraaije, Marco W.
Afiliação
  • Tjallinks G; Molecular Enzymology Group, University of Groningen, Nijenborgh 4, Groningen (The, Netherlands.
  • Boverio A; Department of Biology and Biotechnology, University of Pavia, Via Ferrata 9, Pavia, Italy.
  • Jager AW; Molecular Enzymology Group, University of Groningen, Nijenborgh 4, Groningen (The, Netherlands.
  • Kaya SG; Department of Biology and Biotechnology, University of Pavia, Via Ferrata 9, Pavia, Italy.
  • Mattevi A; Molecular Enzymology Group, University of Groningen, Nijenborgh 4, Groningen (The, Netherlands.
  • Fraaije MW; Molecular Enzymology Group, University of Groningen, Nijenborgh 4, Groningen (The, Netherlands.
Chembiochem ; 24(24): e202300588, 2023 12 14.
Article em En | MEDLINE | ID: mdl-37800383
ABSTRACT
The chemical 5-hydroxymethylfurfural (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 a 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 chemoselective 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 of novel biocatalysts.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Furanos Limite: Animals Idioma: En Revista: Chembiochem Assunto da revista: BIOQUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Holanda

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Furanos Limite: Animals Idioma: En Revista: Chembiochem Assunto da revista: BIOQUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Holanda