Instead of aqueous solutions, universally recognized in enzymology, ternary systems of the waterlorganic solvent/surfactant type are suggested as liquid-crystalline media for enzymatic reactions. Two systems, water/ octane/Aerosol OT and water/cyclohexane/Brij 96, have been used to solubilize acid and alkaline phosphatases and peroxidase. The enzymes under study do function in liquid-crystalline mesophases having lamellar, cylindrical (reversed hexagonal) and ball-shaped (reversed cubic) packing of the surfactant molecules. A significant result is that the phase transition from one liquid-crystalline structure to another entails, as a rule, a reversible change in the catalytic activity of the solubilized enzyme.There is no doubt that the lipid bilayer forms the framework of biological membranes and provides the barrier function [I]. Recently, however, a clear understanding has been achieved of the role that might be played in membranes by lipid polymorphism and local transitions between lamellar (bilayer) and hexagonal lipid phases [2 -171. The topic under discussion is the formation in membranes of hexagonally packed cylinders, in which the polar head groups of lipid molecuies line the narrow channel filled with water. It also seems possible that, inside the lipid bilayer, smaller associates of lipid molecules spring up, almost spherical and built like reversed micelles (lipid particles). The driving forces of such rearrangements in membranes and a possible biological role of non-bilayer structures were discussed in some recent reviews [14, 15,[18][19][20][21][22].These new ideas cause new enzymological problems since the overwhelming majority of enzymes in vivo function on the surface of biological membranes or inside them [23 -301. It is, therefore, important to elicit first whether enzymes can, in principle, possess catalytic activity if they are entrapped into microheterogeneous aggregates (of the types of lamellas, cylinders and/or ball-shaped micelles) built from lipid molecules. Second, whether the catalytic activity of the entrapped enzymes alters after the transition from one type of packing of lipid molecules to another.The problem of lipid dependence of enzymes has long been under discussion [31-401. As the chief regulatory factors (in addition to specific lipid-protein interactions, see for instance [41,42]), the microviscosity [35,39,401 Another regulatory factor might be the capacity of liquid crystals for polymorphism; for review, see monographs [18, 441. Indeed the structural rearrangement of the type : bilayer (L) e hexagonal phase (HI,) was recently found to influence the catalytic activity of some enzymes (phospholipases, phosphodiesterases, ATPase and manosyltransferase) entrapped into proteoliposomes [lo, 45-49] '.In our opinion, a handier way to solve the membranological problems of this kind derives from the solubilization of enzymes in microheterogeneous media of the water/organic solvent/surfactant type [22]. The point is that the amphiphilic molecules of surfactants in water/organ...