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Showing 1–7 of 7 results
Advanced filters: Author: Dörte Rother Clear advanced filters

  • RetroBioCat provides automated solutions for biocatalytic cascade design. The curated open-access tool, developed by researchers in biocatalysis, has the potential to greatly facilitate enzymatic retrosynthesis to target molecules.

    • Dörte Rother
    • Stephan Malzacher
    News & Views
    Nature Catalysis
    Volume: 4, P: 92-93

  • Biocatalysis needs improved reproducibility and quality of research reporting. Our interdisciplinary team has developed a flexible and extensible metadata catalogue based on STRENDA guidelines, essential for describing complex experimental setups in biocatalysis. The catalogue is available online via GitHub for community use.

    • Stephan Malzacher
    • Dominik Meißner
    • Dörte Rother
    Comments & Opinion
    Nature Catalysis
    Volume: 7, P: 1245-1249

  • Peroxygenases can selectively functionalize organic compounds, but are sensitive to the co-substrate H2O2. Hollmann and co-workers show that water oxidation catalysts can provide a controlled supply of H2O2 to the enzyme in the presence of visible light, allowing efficient oxyfunctionalization without stoichiometric reductants.

    • Wuyuan Zhang
    • Elena Fernández-Fueyo
    • Frank Hollmann
    Research
    Nature Catalysis
    Volume: 1, P: 55-62

  • EnzymeML is an XML-based markup language that enables FAIR (findable, accessible, interoperable and reusable) storage and exchange of enzymatic data such as reaction conditions, the time course of the substrate and the product, kinetic parameters and the kinetic model.

    • Simone Lauterbach
    • Hannah Dienhart
    • Jürgen Pleiss
    Research
    Nature Methods
    Volume: 20, P: 400-402

  • Flavin-based biocatalysis using flavin mononucleotide (FMN) cofactor attracts significant attention for its application in asymmetric alkene reduction and various other reactions, however, the scale-up of flavin-based biocatalysis in flow remains unexplored. Here, the authors develop a closed-loop flow platform for H2-driven regeneration of cofactor FMNH2 and ene-reduction using immobilized Old Yellow Enzyme, achieving >99% conversion of ketoisophorone to levodione.

    • Guiyeoul Lim
    • Donato Calabrese
    • Lars Lauterbach
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-7

  • The bio-hybrid fuel 4,5-dimethyl-1,3-dioxolane can be produced from glucose via 2,3-butanediol (2,3-BDO), however, the separation of microbially produced 2,3-BDO remains costly. Here, the authors develop an alternative process route to 4,5-dimethyl-1,3-dioxolane via the enzymatic production of 2,3-BDO.

    • William Graf von Westarp
    • Jan Wiesenthal
    • Andreas Jupke
    ResearchOpen Access
    Communications Chemistry
    Volume: 6, P: 1-11