Jump to main content
Jump to site search

Issue 42, 2019
Previous Article Next Article

Valency engineering of monomeric enzymes for self-assembling biocatalytic hydrogels

Author affiliations

Abstract

All-enzyme hydrogels are efficient reagents for continuous flow biocatalysis. These materials can be obtained by self-assembly of two oligomeric enzymes, modified with the complementary SpyTag and SpyCatcher units. To facilitate access to the large proportion of biocatalytically relevant monomeric enzymes, we demonstrate that the tagging valency of the monomeric (S)-stereoselective ketoreductase Gre2p from Saccharomyces cerevisiae can be designed to assemble stable, active hydrogels with the cofactor-regenerating glucose 1-dehydrogenase GDH from Bacillus subtilis. Mounted in microfluidic reactors, these gels revealed high conversion rates and stereoselectivity in the reduction of prochiral methylketones under continuous flow for more than 8 days. The sequential use as well as parallelization by ‘numbering up’ of the flow reactor modules demonstrate that this approach is suitable for syntheses on the semipreparative scale.

Graphical abstract: Valency engineering of monomeric enzymes for self-assembling biocatalytic hydrogels

Back to tab navigation

Supplementary files

Article information


Submitted
14 Aug 2019
Accepted
30 Aug 2019
First published
06 Sep 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 9752-9757
Article type
Edge Article

Valency engineering of monomeric enzymes for self-assembling biocatalytic hydrogels

P. Bitterwolf, S. Gallus, T. Peschke, E. Mittmann, C. Oelschlaeger, N. Willenbacher, K. S. Rabe and C. M. Niemeyer, Chem. Sci., 2019, 10, 9752
DOI: 10.1039/C9SC04074A

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements