Tandem catalysis in multicomponent solvent-free biofluids

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

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)
62 Downloads (Pure)


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.

Original languageEnglish
Pages (from-to)19797-19805
Number of pages9
Issue number42
Publication statusPublished - 14 Nov 2019


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