ArticleMicrobial biotechnology2022
Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601.
Article in Microbial biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Whole-Cell Biocatalytic Production of 2,5-Furandicarboxylic Acid from 5-Hydroxymethylfurfural byMicroorganisms · 2026Article
- Efficient Whole-Cell Biocatalytic Transformation of Lignin-Derived Syringaldehyde to Syringic Acid with Aryl-Alcohol Oxidase in Deep Eutectic Solvent System.Foods (Basel, Switzerland) · 2026Article
- Article
- Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.Applied microbiology and biotechnology · 2025Review
- Gluconobacter oxydans DSM 50049 - an efficient biocatalyst for oxidation of 5-formyl-2-furancarboxylic acid (FFCA) to 2,5-furandicarboxylic acid (FDCA).Microbial cell factories · 2025Article
- Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade.Scientific reports · 2024Article
- Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601.Microbial biotechnology · 2022Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bio-based 5-hydroxymethylfurfural (HMF) serves as an important platform for several chemicals, among which 2,5-furan dicarboxylic acid (FDCA) has attracted considerable interest as a monomer for the production of polyethylene furanoate (PEF), a potential alternative for fossil-based polyethylene terephthalate (PET). This study is based on the HMF oxidizing activity shown by Mycobacterium sp. MS 1601 cells and investigation of the enzyme catalysing the oxidation. The Mycobacterium whole cells oxidized the HMF to FDCA (60% yield) and hydroxymethyl furan carboxylic acid (HMFCA). A gene encoding a novel bacterial aryl alcohol oxidase, hereinafter MycspAAO, was identified in the genome and was cloned and expressed in Escherichia coli Bl21 (DE3). The purified MycspAAO displayed activity against several alcohols and aldehydes; 3,5 dimethoxy benzyl alcohol (veratryl alcohol) was the best substrate among those tested followed by HMF. 5-Hydroxymethylfurfural was converted to 5-formyl-2-furoic acid (FFCA) via diformyl furan (DFF) with optimal activity at pH 8 and 30-40°C. FDCA formation was observed during long reaction time with low HMF concentration. Mutagenesis of several amino acids shaping the active site and evaluation of the variants showed Y444F to have around 3-fold higher k
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