Recreating some of the emergent behavior seen in biological reaction networks is an important goal in the new field of systems chemistry. One of the classic examples of complex behavior is bistability, which is abundantly used in living organisms for switching between cellular states. Here, we create a bistable switch based on the autocatalytic activation and inhibition of the enzyme trypsin under flow conditions. We investigate the influence of the inhibitor structure, and hence inhibition kinetics, on the properties of the bistable switch.
