Design of Fusion Enzymes for Biocatalytic Applications in Aqueous and Non-aqueous Media

Yu Ma, Ningning Zhang, Guillem Vernet, Selin Kara*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

14 Citations (Scopus)

Abstract

Biocatalytic cascades play a fundamental role in sustainable chemical synthesis. Fusion enzymes are one of the powerful toolboxes to enable the tailored combination of multiple enzymes for efficient cooperative cascades. Especially, this approach offers a substantial potential for the practical application of cofactor-dependent oxidoreductases by forming cofactor self-sufficient cascades. Adequate cofactor recycling while keeping the oxidized/reduced cofactor in a confined microenvironment benefits from the fusion fashion and makes the use of oxidoreductases in harsh non-aqueous media practical. In this mini-review, we have summarized the application of various fusion enzymes in aqueous and non-aqueous media with a focus on the discussion of linker design within oxidoreductases. The design and properties of the reported linkers have been reviewed in detail. Besides, the substrate loadings in these studies have been listed to showcase one of the key limitations (low solubility of hydrophobic substrates) of aqueous biocatalysis when it comes to efficiency and economic feasibility. Therefore, a straightforward strategy of applying non-aqueous media has been briefly discussed while the potential of using the fusion oxidoreductase of interest in organic media was highlighted.

Original languageEnglish
Article number944226
JournalFrontiers in Bioengineering and Biotechnology
Volume10
Number of pages11
ISSN2296-4185
DOIs
Publication statusPublished - Jul 2022

Keywords

  • aqueous and non-aqueous media
  • biocatalytic cascades
  • fusion enzymes
  • fusion linkers
  • oxidoreductases
  • PROTEIN
  • LINKER LENGTH
  • ENZYMATIC CATALYSIS
  • BAEYER-VILLIGER OXIDATION
  • CASCADE
  • EN-ROUTE
  • MONOOXYGENASE
  • EPSILON-CAPROLACTONE
  • MICROBIAL TRANSFORMATIONS
  • ALCOHOL-DEHYDROGENASE

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