Enzymes can activate and mobilize dense biomolecular condensates across scales.

Condensed enzymes show faster catalysis in protein-crowded droplets, where enzymatic activity increases diffusion and macroscopic flow despite crowding that might raise viscosity.

• Why it matters: Condensate enzymatic activity is largely unexplored because metabolism-driven, non-equilibrium behavior is hard to integrate with phase separation dynamics.
• What they did: Using experimental, computational, and theoretical methods, the study links catalytic non-equilibrium activity to environmental feedback across five orders of magnitude of length scales.
• The result: The enhanced activity is attributed to lower-energy protein conformations induced by crowding, making droplets more agile via diffusion and macroscopic flow, informing metabolically active liquid-liquid phase separation.

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