Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade
Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O2 to H2O2. Their activity on furan derivatives like 5-hydroxymethylfurfural (HMF) makes these enzymes promising biocatalysts for the environmentally friendly synthesis o...
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ftyyuniv:ebff6ec7-4720-460c-8661-7008332dd62d 2024-09-15T17:48:47+00:00 Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade Jankowski, Nina Koschorreck, Katja Urlacher, Vlada B. Alpdağtaş, Saadet 2024-12-01T00:00:00Z https://doi.org/10.1038/s41598-024-56429-z https://avesis.yyu.edu.tr/publication/details/ebff6ec7-4720-460c-8661-7008332dd62d/oai eng eng ebff6ec7-4720-460c-8661-7008332dd62d doi:10.1038/s41598-024-56429-z https://avesis.yyu.edu.tr/publication/details/ebff6ec7-4720-460c-8661-7008332dd62d/oai info:eu-repo/semantics/openAccess info:eu-repo/semantics/article 2024 ftyyuniv https://doi.org/10.1038/s41598-024-56429-z 2024-08-16T04:04:38Z Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O2 to H2O2. 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). TvGLOX was found to catalyze the oxidation of aldehyde groups in glyoxylic acid, methyl glyoxal, HMF, 2,5-diformylfuran (DFF) and 5-formyl-2-furancarboxylic acid (FFCA), but barely accepted alcohol groups as in 5-hydroxymethyl-2-furancarboxylic acid (HMFCA), preventing formation of FDCA from HMF. Various redox activators were tested for TvGLOX reactivation during catalyzed reactions. Among them, a combination of horseradish peroxidase and its substrate 2,2′-azino-di-(3-ethylbenzthiazoline sulfonic acid) (ABTS) most efficiently reactivated TvGLOX. Through continuous reactivation of TvGLOX in a two-enzyme system employing a recombinant Moesziomyces antarcticus aryl-alcohol oxidase (MaAAO) almost complete conversion of 8 mM HMF to FDCA was achieved within 24 h. Article in Journal/Newspaper Antarc* antarcticus Van Yüzüncü Yıl University Research Information System Scientific Reports 14 1 |
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Van Yüzüncü Yıl University Research Information System |
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English |
description |
Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O2 to H2O2. 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). TvGLOX was found to catalyze the oxidation of aldehyde groups in glyoxylic acid, methyl glyoxal, HMF, 2,5-diformylfuran (DFF) and 5-formyl-2-furancarboxylic acid (FFCA), but barely accepted alcohol groups as in 5-hydroxymethyl-2-furancarboxylic acid (HMFCA), preventing formation of FDCA from HMF. Various redox activators were tested for TvGLOX reactivation during catalyzed reactions. Among them, a combination of horseradish peroxidase and its substrate 2,2′-azino-di-(3-ethylbenzthiazoline sulfonic acid) (ABTS) most efficiently reactivated TvGLOX. Through continuous reactivation of TvGLOX in a two-enzyme system employing a recombinant Moesziomyces antarcticus aryl-alcohol oxidase (MaAAO) almost complete conversion of 8 mM HMF to FDCA was achieved within 24 h. |
format |
Article in Journal/Newspaper |
author |
Jankowski, Nina Koschorreck, Katja Urlacher, Vlada B. Alpdağtaş, Saadet |
spellingShingle |
Jankowski, Nina Koschorreck, Katja Urlacher, Vlada B. Alpdağtaş, Saadet Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
author_facet |
Jankowski, Nina Koschorreck, Katja Urlacher, Vlada B. Alpdağtaş, Saadet |
author_sort |
Jankowski, Nina |
title |
Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
title_short |
Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
title_full |
Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
title_fullStr |
Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
title_full_unstemmed |
Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade |
title_sort |
identification of redox activators for continuous reactivation of glyoxal oxidase from trametes versicolor in a two-enzyme reaction cascade |
publishDate |
2024 |
url |
https://doi.org/10.1038/s41598-024-56429-z https://avesis.yyu.edu.tr/publication/details/ebff6ec7-4720-460c-8661-7008332dd62d/oai |
genre |
Antarc* antarcticus |
genre_facet |
Antarc* antarcticus |
op_relation |
ebff6ec7-4720-460c-8661-7008332dd62d doi:10.1038/s41598-024-56429-z https://avesis.yyu.edu.tr/publication/details/ebff6ec7-4720-460c-8661-7008332dd62d/oai |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1038/s41598-024-56429-z |
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Scientific Reports |
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14 |
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