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Cascade Kinetics in an Enzyme-Loaded Aqueous Two-Phase System.

Marko Pavlovic1, Alexander Plucinski1,2, Jianrui Zhang1

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Macromolecular crowding in aqueous two-phase systems (ATPS) influences enzyme kinetics. Ion hydration affects protein partitioning, enabling control over enzymatic cascade reactions for synthetic protocells.

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Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Physical Chemistry

Background:

  • Macromolecular crowding is crucial for enzymatic reaction kinetics.
  • Liquid-liquid phase separation in cells creates dynamic compartments, affecting enzyme concentration and substrate diffusion.
  • Aqueous two-phase systems (ATPS) mimic cellular environments for studying enzyme behavior.

Purpose of the Study:

  • To investigate the partitioning of enzymes (horseradish-peroxidase, urate-oxidase) in a poly(ethylene glycol)-dextran ATPS.
  • To analyze the influence of salt concentration and Hofmeister series ions on enzyme partitioning and kinetics.
  • To explore enzymatic cascade reactions within ATPS for controlled reactivity.

Main Methods:

  • Utilized a poly(ethylene glycol)-dextran aqueous two-phase system (ATPS).
  • Varied salt concentration and ion type (Hofmeister series) to study protein partitioning.
  • Investigated enzymatic cascade reactions and kinetics within the ATPS.

Main Results:

  • Protein partitioning in ATPS is strongly influenced by ion hydration, following the Hofmeister series.
  • Achieved cross-partitioning of two enzymes by exploiting differences in net protein charge at a specific pH.
  • Enzyme activity and reaction kinetics in ATPS depend on substrate type and crowding agent interactions.

Conclusions:

  • Ion hydration significantly modulates enzyme partitioning and kinetics in crowded ATPS environments.
  • ATPS provides a tunable platform for controlling enzymatic cascade reactions.
  • Findings have implications for designing dynamic regulatory mechanisms in synthetic protocells.