ArticleChemSusChem2025
A Simple Strategy for Co-Immobilization of NADH-Dependent Enzymes and NADH for Efficient Biocatalysis in Continuous Flow Reactors.
Article in ChemSusChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Review
- Carrier-Free Enzyme Immobilization for High-Density Catalytic Architectures in Flow Biocatalysis.JACS Au · 2026Review
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Authors and funding
4 authors.
Funding
Abstract
The application of nicotinamide adenine dinucleotide (NAD)(H)-dependent enzymes in continuous flow reactors poses significant challenges due to the high cost of NAD(H) and its inevitable loss during reactor operation. To overcome these limitations, a novel platform comprising Cry3Aa-enzyme fusion particles modified with polyethylenimine (PEI) is developed and its application for two catalytic processes is demonstrated. In the first system, two NAD(H)-dependent enzymes, formate dehydrogenase (FDH), and leucine dehydrogenase (LDH) are genetically co-immobilized within Cry3Aa particles and then modified with PEI to facilitate NADH co-immobilization. To adapt the system for continuous flow reactors, PEI-modified particles are entrapped within agarose beads, loaded with NADH, and then used to catalyze L-tert leucine production under continuous flow conditions for 30 days. This configuration achieved LDH and NADH turnover numbers of 22,196 and 7,202, respectively, and a space-time yield (STY) of 0.0262 g L
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