biostudies-literatureAlruwaili AFP7 Joint Technology InitiativesNorthern Border UniversityBiotechnology and Biological Sciences Research Council3549-3560https://www.ebi.ac.uk/biostudies/studies/S-EPMC10167727biostudies-literatureUnknown25(9)Lignin oxidation by bacterial dye-decolorizing peroxidase enzymes requires hydrogen peroxide as a co-substrate, an unstable and corrosive oxidant. We have identified a glycolate oxidase enzyme from <i>Rhodococcus jostii</i> RHA1 that can couple effectively at pH 6.5 with DyP peroxidase enzymes from <i>Agrobacterium</i> sp. or <i>Comamonas testosteroni</i> to oxidise lignin substrates without addition of hydrogen peroxide. <i>Rhodococcus jostii</i> RHA1 glycolate oxidase (RjGlOx) has activity for oxidation of a range of α-ketoaldehyde and α-hydroxyacid substrates, and is also active for oxidation of hydroxymethylfurfural (HMF) to furandicarboxylic acid. The combination of RjGlOx with <i>Agrobacterium</i> sp. DyP or <i>C. testosteroni</i> DyP generated new and enhanced amounts of low moleculGreen chemistry : an international journal and green chemistry resource : GCApplication of <i>Rhodococcus jostii</i> RHA1 glycolate oxidase as an efficient accessory enzyme for lignin conversion by bacterial Dyp peroxidase enzymes.PMC10167727Grant Agreement 720303BB/T010622/1Rashid GMMAlruwaili ABugg TDHfalseApplication of <i>Rhodococcus jostii</i> RHA1 glycolate oxidase as an efficient accessory enzyme for lignin conversion by bacterial Dyp peroxidase enzymes.Lignin oxidation by bacterial dye-decolorizing peroxidase enzymes requires hydrogen peroxide as a co-substrate, an unstable and corrosive oxidant. We have identified a glycolate oxidase enzyme from <i>Rhodococcus jostii</i> RHA1 that can couple effectively at pH 6.5 with DyP peroxidase enzymes from <i>Agrobacterium</i> sp. or <i>Comamonas testosteroni</i> to oxidise lignin substrates without addition of hydrogen peroxide. <i>Rhodococcus jostii</i> RHA1 glycolate oxidase (RjGlOx) has activity for oxidation of a range of α-ketoaldehyde and α-hydroxyacid substrates, and is also active for oxidation of hydroxymethylfurfural (HMF) to furandicarboxylic acid. The combination of RjGlOx with <i>Agrobacterium</i> sp. DyP or <i>C. testosteroni</i> DyP generated new and enhanced amounts of low molecul2023-01-01T00:00:00Z2023 May2026-07-14T20:07:41.686Z2025-04-06T14:33:40.146ZS-EPMC101677273717995810.1039/d3gc00475a