Experimental approaches to modelling the enzymatic function of biological membranes are discussed. Emphasis is given to pseudohomogeneous systems such as proteolipid complexes and enzymes in organic solvents; the latter are solubilized with phospholipids or synthetic surfactants. Methods for producing and studying such micellar systems are considered. The key research problems of micellar enzymology are formulated and its relation to enzyme membranology is discussed. Finally, the new potentialities are noted of applied enzymology (biotechnology) offered by application of a colloidal solution of water in organic solvents as a microheterogeneous medium for enzymatic reactions.Until now the development of molecular enzymology has been mainly directed to studying free enzymes [l -41. In other words, the most valuable experiments aimed at elucidating the structure of catalytic centers and the physico-chemical mechanisms of biocatalysis were successful only with the enzymes isolated from the living cells in quite a pure form. However, such 'pure' experiments, as was noted time and again [5], naturally raise the question as to whether the enzyme properties observed in vitro can be correlated adequately with the conditions of its functioning in vivo. Such a doubt is quite equitable since it became clear [6 -91 that the subcellular structure and the compartmentalization of enzymes play the most important role in metabolism regulation.Thus, the essence of the contradiction is that in vitro studies of enzymes are usually conducted in water (buffer). However, in the living cell, enzymes mostly act on or near the 'water/ organic medium' interface. For instance, many enzymes, if not the majority, are located on the surface of biological membranes or inside them [lo-161. Other enzymes function in mobile complexes with macromolecular components of the cell, e.g. with proteins or polysaccharides [14 -161. Generally speaking, the boundary between 'bound' and 'diffusion-free' enzymes is rather conventional, and such a classification is more methodical (depending on the ease of the enzyme isolation) than functional (the enzyme localization in the cell) [16]. The problem is that many of the enzymes bind to the membrane surface loosely and the degree of their binding depends on the concentration of metabolites [14-191. The physiological state of the cell determines not only the adsorption of some enzymes but their possible translocation through membranes [20,21]. In the adsorbed state in vivo (on the enterocyte brushborder) extracellular enzymes were found as well, such as proteases of the digestive tract, namely trypsin and a-chymotrypsin [22, 231, which up to now have remained model subjects of the classical 'in-water' enzymology.Finally, a few words about the medium in which diffusionfree enzymes function in the cell (for a review see [24]). It is not very clear why macromolecules (immunoglobulins and albumin) injected into the living cell diffuse so slowly (as in a 60% sucrose solution) [25]. The comparison of the diffusion rat...

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To simulate in vitro the conditions under which enzymes act in vivo, enzyme molecules have been entrapped in hydrated reverse micelles of a surfactant in organic solvents. In this system the catalytic activity of one of the enzymes studied (peroxidase) became much higher than in water, and the specificity of the other enzyme (alcohol dehydrogenase) was dramatically altered.