ArticleBiotechnology for biofuels2018
Creating a more robust 5-hydroxymethylfurfural oxidase by combining computational predictions with a novel effective library design.
Article in Biotechnology for biofuels, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 63 citations in OpenAlex.
- Immobilized Hydroxymethylfurfural Oxidase Enables Robust Biocatalytic Production of 2,5-Furandicarboxylic Acid from Crude 5‑Hydroxymethylfurfural.ACS sustainable chemistry & engineering · 2026Article
- Advance biocatalyst for the green conversion of 5-hydroxymethylfurfural to a biopolymer precursor 2,5-furandicarboxylic acid.Biotechnology for biofuels and bioproducts · 2025Article
- Article
- Enriching stabilizing mutations through automated analysis of molecular dynamics simulations using BoostMut.Protein science : a publication of the Protein Society · 2025Article
- In Vivo Biocatalytic Cascades Featuring an Artificial-Enzyme-Catalysed New-to-Nature Reaction.Angewandte Chemie (International ed. in English) · 2023Article
- Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound.Nature communications · 2022Article
- Optimizing operational parameters for the enzymatic production of furandicarboxylic acid building block.Microbial cell factories · 2021Article
- Toward scalable biocatalytic conversion of 5-hydroxymethylfurfural by galactose oxidase using coordinated reaction and enzyme engineering.Nature communications · 2021Article
- Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production.Applied and environmental microbiology · 2020Article
- Article
- Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase.Angewandte Chemie (International ed. in English) · 2020Article
- Robust ω-Transaminases by Computational Stabilization of the Subunit Interface.ACS catalysis · 2020Article
- Stabilization of cyclohexanone monooxygenase by computational and experimental library design.Biotechnology and bioengineering · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHMF oxidase (HMFO) from
resultsTo increase the robustness of HMFO, a requirement for biotechnological applications, we decided to enhance its thermostability using the recently developed FRESCO method: a computational approach to identify thermostabilizing mutations in a protein structure. To make this approach even more effective, we now developed a new and facile gene shuffling approach to rapidly combine stabilizing mutations in a one-pot reaction. This allowed the identification of the optimal combination of seven beneficial mutations. The created thermostable HMFO mutant was further studied as a biocatalyst for the production of FDCA from HMF and was shown to perform significantly better than the original HMFO.
conclusionsThe described new gene shuffling approach quickly discriminates stable and active multi-site variants. This makes it a very useful addition to FRESCO. The resulting thermostable HMFO variant tolerates the presence of cosolvents and also remained thermotolerant after introduction of additional mutations aimed at improving the catalytic activity. Due to its stability and catalytic efficiency, the final HMFO variant appears to be a promising candidate for industrial scale production of FDCA from HMF.
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