<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14(1)</volume><submitter>Alpdagtas S</submitter><funding>Scientific and Technological Research Council of Turkey</funding><funding>Heinrich-Heine-Universität Düsseldorf</funding><funding>Ministry of Innovation, Science and Research of the German State of North Rhine-Westphalia</funding><pubmed_abstract>Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O&lt;sub>2&lt;/sub> to H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>. Their activity on furan derivatives like 5-hydroxymethylfurfural (HMF) makes these enzymes promising biocatalysts for the environmentally friendly synthesis of the bioplastics precursor 2,5-furandicarboxylic acid (FDCA). However, glyoxal oxidases suffer from inactivation, which requires the identification of suitable redox activators for efficient substrate conversion. Furthermore, only a few glyoxal oxidases have been expressed and characterized so far. Here, we report on a new glyoxal oxidase from Trametes versicolor (TvGLOX) that was expressed at high levels in Pichia pastoris (reclassified as Komagataella phaffii)</pubmed_abstract><journal>Scientific reports</journal><pagination>5932</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10928124</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade.</pubmed_title><pmcid>PMC10928124</pmcid><pubmed_authors>Urlacher VB</pubmed_authors><pubmed_authors>Jankowski N</pubmed_authors><pubmed_authors>Koschorreck K</pubmed_authors><pubmed_authors>Alpdagtas S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade.</name><description>Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O&lt;sub>2&lt;/sub> to H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>. Their activity on furan derivatives like 5-hydroxymethylfurfural (HMF) makes these enzymes promising biocatalysts for the environmentally friendly synthesis of the bioplastics precursor 2,5-furandicarboxylic acid (FDCA). However, glyoxal oxidases suffer from inactivation, which requires the identification of suitable redox activators for efficient substrate conversion. Furthermore, only a few glyoxal oxidases have been expressed and characterized so far. Here, we report on a new glyoxal oxidase from Trametes versicolor (TvGLOX) that was expressed at high levels in Pichia pastoris (reclassified as Komagataella phaffii)</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Mar</publication><modification>2026-07-15T04:35:17.749Z</modification><creation>2024-11-15T12:26:34.217Z</creation></dates><accession>S-EPMC10928124</accession><cross_references><pubmed>38467766</pubmed><doi>10.1038/s41598-024-56429-z</doi></cross_references></HashMap>