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Beneficial substrate partitioning boosts non-aqueous catalysis in de novo enzyme-alginate beads

Richard Stenner, View ORCID ProfileH. Adrian Bunzel, View ORCID ProfileAdrian J. Mulholland, View ORCID ProfileJ. L. Ross Anderson
doi: https://doi.org/10.1101/2021.04.12.439416
Richard Stenner
†School of Biochemistry, University of Bristol, University Walk, BS8 1TD Bristol, UK
‡Bristol Centre for Functional Nanomaterials, HH Wills Physics Laboratory, University of Bristol, BS8 1TL Bristol, UK
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H. Adrian Bunzel
†School of Biochemistry, University of Bristol, University Walk, BS8 1TD Bristol, UK
§Centre for Computational Chemistry, School of Chemistry, University of Bristol, BS8 1TS Bristol, UK
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  • ORCID record for H. Adrian Bunzel
Adrian J. Mulholland
§Centre for Computational Chemistry, School of Chemistry, University of Bristol, BS8 1TS Bristol, UK
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J. L. Ross Anderson
†School of Biochemistry, University of Bristol, University Walk, BS8 1TD Bristol, UK
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  • ORCID record for J. L. Ross Anderson
  • For correspondence: ross.anderson@bristol.ac.uk
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ABSTRACT

Synthetic reactions often involve solvents incompatible with biocatalysts. Here, we encapsulate de novo heme-containing enzymes in calcium-alginate beads to facilitate heterogeneous biocatalysis in organic solvents. After encapsulation, enzymes remained structured and retained activity even when the beads are suspended in organic solvents. Carbene transferase activity, brought about by the heme cofactor, was enhanced when reactions were performed in organic solvent with alginate-encapsulated enzymes. Activity-solvent dependencies revealed that the activity boost is due to beneficial partitioning of the substrate between the beads and organic phase. Encapsulation furthermore facilitates enzyme recycling after the reaction. Alginate encapsulation opens up novel opportunities for biocatalysis in organic solvent systems, combining desired solvent properties of organic chemistry with enzymatic selectivity and proficiency.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted April 12, 2021.
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Beneficial substrate partitioning boosts non-aqueous catalysis in de novo enzyme-alginate beads
Richard Stenner, H. Adrian Bunzel, Adrian J. Mulholland, J. L. Ross Anderson
bioRxiv 2021.04.12.439416; doi: https://doi.org/10.1101/2021.04.12.439416
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Beneficial substrate partitioning boosts non-aqueous catalysis in de novo enzyme-alginate beads
Richard Stenner, H. Adrian Bunzel, Adrian J. Mulholland, J. L. Ross Anderson
bioRxiv 2021.04.12.439416; doi: https://doi.org/10.1101/2021.04.12.439416

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