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Showing 1–7 of 7 results
Advanced filters: Author: Peter Westh Clear advanced filters

  • The 1913 study ‘Die Kinetik der Invertinwirkung’, by Michaelis and Menten, marked a pivotal advancement in enzymology by illustrating the application of mechanistic models and quantitative kinetics to biocatalysis. The foundational framework described back then continues to have a strong impact on enzymology, with profound influences that range from undergraduate education to structure–function studies and the format and content of contemporary kinetic databases.

    • Peter Westh
    • Jeppe Kari
    News & Views
    Nature Catalysis
    Volume: 8, P: 859-860

  • Biosensors are powerful tools for quantification of a wide range of molecules but require extensive engineering for each analyte. Here, the authors engineered a robust environmental bacterium for sensing a diverse set of chemicals, such as lactate and PET degradation products, via growth-coupling

    • Javier M. Hernández-Sancho
    • Arnaud Boudigou
    • Pablo I. Nikel
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Enzymatic depolymerization of polyethylene terephthalate (PET) towards monomer recycling is a promising strategy for a bio-based circular plastic economy, but progress is limited by the lack of standard guidelines for assessing and comparing the depolymerization efficiency catalysed by various PET hydrolases. In this Perspective, the authors identify critical research gaps in sourcing novel PET hydrolases and specify crucial requirements for selecting and optimizing them for specific application scenarios.

    • Ren Wei
    • Peter Westh
    • Uwe T. Bornscheuer
    ReviewsOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • Enzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a so-called linear free energy relationship, which may help rationalize cellulolytic mechanisms and guide the selection of technical enzymes.

    • Jeppe Kari
    • Gustavo A. Molina
    • Peter Westh
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10

  • Glucuronoyl esterases have the potential to be used in the biocatalytic conversion of lignin-carbohydrate complexes to obtain pure lignin for downstream biofuel conversion. Here the authors present a detailed structural analysis of the glucuronoyl esterase from Cerrena unicolor, providing the basis for its activity on natural substrate and for how lignin can be selectively separated from lignocellulosic materials.

    • Heidi A. Ernst
    • Caroline Mosbech
    • Sine Larsen
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12