ArticleNature communications2025
Enhanced enzyme stability at the interphase of water-oil for continuous-flow olefin epoxidation.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Compartmentalized Liquid Microenvironments of Pickering Emulsion Droplets for Continuous-Flow Catalysis.JACS Au · 2026Review
- Nanomaterial Integration at Liquid-Liquid Interfaces for Green Catalysis.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Porous Functional Nanomaterials for Continuous Flow Catalysis.Nano-micro letters · 2026Review
- Article
- Nature-Inspired Enzymatic Cascades: Emerging Strategies for Sustainable Chemistry.Molecules (Basel, Switzerland) · 2026Review
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Authors and funding
10 authors.
Funding
Abstract
The practical applications of enzymes often require their immobilization for multiple recycling or long-term running. However, practically efficient enzyme immobilization methods are lacking. Herein, we present an enzyme immobilization approach by engineering a porous "interphase" between water and oil around the surfaces of Pickering emulsion droplets. The designed "interphase" consists of a porous, nanometer-thick silica shell serving as a scaffold to incorporate enzymes. Within this "interphase", enzymes can simultaneously be in contact with enzyme-preferred aqueous microenvironment and the oil phase containing organic reactants. The porous "interphase" with its tunable structure and properties allows modulation of transport of reactants, crudely akin to a cell membrane, and of local concentration of reactants. As a proof of the concept, we showcase that our "interphase" strategy is very effective in immobilization of Candida antarctica lipase B (CALB) for continuous-flow olefin epoxidation. Long-term stabilization (800 h), 16-fold increase in catalysis efficiency relative to batch reactions, and 99% H
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