ArticleChemSusChem2026
Extending Cofactor-Tethered Nanomachines to Complex Multienzyme Redox Cascades in Continuous Flow.
Article in ChemSusChem, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
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Abstract
Multienzyme cascades are emerging as alternatives to fermentation for converting biogenic feedstocks into value-added chemicals and fuels. A major bottleneck in redox transformations is the loss of costly and unstable cofactors in continuous-flow systems, typically necessitating co-immobilization and complex regeneration schemes. Self-sufficient biocatalytic nanomachines, created by fusing enzymes with tethered cofactors, offer a streamlined solution by enabling intramolecular cofactor retention and recycling. Here, we demonstrate that such nanomachines can be integrated into a complete redox-dependent cascade, exemplified by a 10-step glucose-to-isobutanol pathway. Oxidoreductases were fused into redox pairs using peptide linkers containing a single cysteine for covalent attachment of polyethylene glycol (PEG)-modified nicotinamide cofactors, with rational selection of monomeric enzymes ensuring structural compatibility and soluble expression. The resulting nanomachines remained catalytically competent and produced isobutanol in both batch and continuous-flow operation without the addition of free NAD
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