Controlling membrane permeability with bacterial porins: application to encapsulated enzymes.

Recent achievements of membrane protein science allow easy protein modification by genetic engineering and, for some proteins, their production in large quantities. We regard these features as the basic requirements for applications of membrane proteins in materials science. Here, we demonstrate a possible application of membrane proteins, inserting porins from the outer cell wall of Escherichia coli into the walls of liposomes. Encapsulation of enzymes into liposomes or polymer nanocapsules protects them against proteases and denaturation. Functional reconstitution of porins into the capsule shell allows to control the rate and selectivity of substrate permeation, and thus to control the enzyme reaction kinetics. We suggest that this technique can prove to be useful in the area of biosensors, providing enzymatic stability while keeping the functionality or even enhancing the sensitivity by substrate preselection. Another application of this kind of stabilisation is in the field of single enzyme activity recording.