ArticleLangmuir : the ACS journal of surfaces and colloids2020
Cascade Kinetics in an Enzyme-Loaded Aqueous Two-Phase System.
Article in Langmuir : the ACS journal of surfaces and colloids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 43 citations in OpenAlex.
- Dynamic and Catalytic Multiphase Coacervates.Biomacromolecules · 2026Article
- Nature-Inspired Enzymatic Cascades: Emerging Strategies for Sustainable Chemistry.Molecules (Basel, Switzerland) · 2026Review
- Advancements in Aqueous Two-Phase Systems for Enzyme Extraction, Purification, and Biotransformation.Molecules (Basel, Switzerland) · 2024Review
- Thermo-responsive aqueous two-phase system for two-level compartmentalization.Nature communications · 2024Article
- Review
- Uricase Crowding via Polyelectrolyte Layers Coacervation for Carbon Fiber-Based Electrochemical Detection of Uric Acid.Polymers · 2022Article
- Attomolar Sensitivity in Single Biomarker Counting upon Aqueous Two-Phase Surface Enrichment.ACS sensors · 2022Article
- Masks Start to Drop: Suppressor of MAX2 1-Like Proteins Reveal Their Many Faces.Frontiers in plant science · 2022Review
- Biological Phase Separation and Biomolecular Condensates in Plants.Annual review of plant biology · 2021Review
- Exploring New Horizons in Liquid Compartmentalization via Microfluidics.Biomacromolecules · 2021Article
- Addressing the Selectivity of Enzyme Biosensors: Solutions and Perspectives.Sensors (Basel, Switzerland) · 2021Review
- The role of liquid-liquid phase separation in regulating enzyme activity.Current opinion in cell biology · 2021Review
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6 authors at 1 institution in 2 countries.
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Abstract
Macromolecular crowding plays a critical role in the kinetics of enzymatic reactions. Dynamic compartmentalization of biological components in living cells due to liquid-liquid phase separation represents an important cell regulatory mechanism that can increase enzyme concentration locally and influence the diffusion of substrates. In the present study, we probed partitioning of two enzymes (horseradish-peroxidase and urate-oxidase) in a poly(ethylene glycol)-dextran aqueous two-phase system (ATPS) as a function of salt concentration and ion position in the Hofmeister series. Moreover, we investigated enzymatic cascade reactions and their kinetics within the ATPS, which revealed a strong influence of the ion hydration stemming from the background electrolyte on the partitioning coefficients of proteins following the Hofmeister series. As a result, we were able to realize cross-partitioning of two enzymes because of different protein net charges at a chosen pH. Our study reveals a strong dependency of the enzyme activity on the substrate type and crowding agent interaction on the final kinetics of enzymatic reactions in the ATPS and therefore provides substantial implications en route toward dynamic regulation of reactivity in synthetic protocells.
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