{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alruwaili A"],"funding":["FP7 Joint Technology Initiatives","Northern Border University","Biotechnology and Biological Sciences Research Council"],"pagination":["3549-3560"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10167727"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(9)"],"pubmed_abstract":["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 molecul"],"journal":["Green chemistry : an international journal and green chemistry resource : GC"],"pubmed_title":["Application of <i>Rhodococcus jostii</i> RHA1 glycolate oxidase as an efficient accessory enzyme for lignin conversion by bacterial Dyp peroxidase enzymes."],"pmcid":["PMC10167727"],"funding_grant_id":["Grant Agreement 720303","BB/T010622/1"],"pubmed_authors":["Rashid GMM","Alruwaili A","Bugg TDH"],"additional_accession":[]},"is_claimable":false,"name":"Application of <i>Rhodococcus jostii</i> RHA1 glycolate oxidase as an efficient accessory enzyme for lignin conversion by bacterial Dyp peroxidase enzymes.","description":"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 molecul","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-07-14T20:07:41.686Z","creation":"2025-04-06T14:33:40.146Z"},"accession":"S-EPMC10167727","cross_references":{"pubmed":["37179958"],"doi":["10.1039/d3gc00475a"]}}