Microbial β-etherases and glutathione lyases for lignin valorisation in biorefineries: current state and future perspectives

Appl Microbiol Biotechnol. 2018 Jul;102(13):5391-5401. doi: 10.1007/s00253-018-9040-3. Epub 2018 May 4.

Abstract

Lignin is the major aromatic biopolymer in nature, and it is considered a valuable feedstock for the future supply of aromatics. Hence, its valorisation in biorefineries is of high importance, and various chemical and enzymatic approaches for lignin depolymerisation have been reported. Among the enzymes known to act on lignin, β-etherases offer the possibility for a selective cleavage of the β-O-4 aryl ether bonds present in lignin. These enzymes, together with glutathione lyases, catalyse a reductive, glutathione-dependent ether bond cleavage displaying high stereospecificity. β-Etherases and glutathione lyases both belong to the superfamily of glutathione transferases, and several structures have been solved recently. Additionally, different approaches for their application in lignin valorisation have been reported in the last years. This review gives an overview on the current knowledge on β-etherases and glutathione lyases, their biochemical and structural features, and critically discusses their potential for application in biorefineries.

Keywords: Biomass valorisation; Ether bond cleavage; Glutathione lyase; Lignin; β-O-4 aryl ether; β-etherase.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins / metabolism*
  • Bioreactors*
  • Lignin / metabolism*
  • Lyases / metabolism*
  • Oxidoreductases / metabolism*

Substances

  • Bacterial Proteins
  • Lignin
  • Oxidoreductases
  • aryl ether cleaving enzyme
  • Lyases