Abstract
We present a thermodynamically consistent model describing the dynamics of a multicomponent mixture where one enzyme component catalyzes a reaction between other components. We find that the catalytic activity alone can induce phase separation for sufficiently active systems and large enzymes, without any equilibrium interactions between components. In the limit of fast reaction rates, binodal lines can be calculated using a mapping to an effective free energy. We also explain how this catalysis-induced phase separation can act to autoregulate the enzymatic activity, which points at the biological relevance of this phenomenon.
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