Tandem catalysis in multicomponent solvent-free biofluids

Dylan Luke Atkins (Corresponding author), José Augusto Berrocal, Alexander Francesco Mason, Ilja Karina Voets

    Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikelAcademicpeer review

    3 Citaten (Scopus)
    43 Downloads (Pure)

    Samenvatting

    Enzymes are widely employed to reduce the environmental impact of chemical industries as biocatalysts improve productivity and offer high selectively under mild reaction conditions in a diverse range of chemical transformations. The poor stability of biomacromolecules under reaction conditions is often a critical bottleneck to their application. Protein engineering or immobilization onto solid substrates may remedy this limitation but, unfortunately, this is often at the expense of catalytic potency or substrate specificity. In this work, we show that the combinatorial approach of chemical modification and supramolecular nanoencapsulation can endow mechanistically diverse enzymes with apparent extremophilic behavior. A protein-polymer surfactant core-shell architecture facilitates construction of increasingly complex biofluids from individual biosynthetic components, each of which retain biological activity at hydration levels almost two orders of magnitude below solvation. The herein constructed multifunctional biofluids operate in tandem up to 150 °C and in the total absence of solvent under apparent diffusional mass-transport limitation. The biosynthetic promotion of extremophilic traits for enzymes with diverse catalytic motions and chemical functions highlights the extraordinary capacity for a viscous surfactant milieu to replace both hydration and bulk waters.

    Originele taal-2Engels
    Pagina's (van-tot)19797-19805
    Aantal pagina's9
    TijdschriftNanoscale
    Volume11
    Nummer van het tijdschrift42
    DOI's
    StatusGepubliceerd - 14 nov 2019

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