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Protein Engineering vol. 4 no. 8 pp. 1009-1017, 1991
© 1991 Oxford University Press

RESEARCH-ARTICLE

Engineering of functional supramacromolecular complexes of proteins (enzymes) using reversed micelles as matrix microreactors

Alexander V. Kabanov, Natalya L. Klyachko, Sergei N. Nametkin, Steffen Merker1,2, Anna V. Zaroza1, Vita I. Bunik3, Mikhail V. Ivanov and Andrey V. Levashov

Department of Chemical Enzymology, Faculty of Chemistry, M.V. Lomonosov Moscow State University 119899, GSP, USSR 1Department of Biochemistry, Faculty of Biology, M.V. Lomonosov Moscow State University Moscow, 119899, GSP, USSR 2Present address: Research Centre of Biotechnology Alt Stralau 62, Berlin, 1017, Germany 3A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, M.V. Lomonosov Moscow State University Moscow, 119899, GSP, USSR

The size of the inner water cavity of reversed micelles formed in a triple system ‘water-surfactant-organic solvent’ can be widely varied by changing the degree of surfactant hydration. This gives grounds to use reversed micelles as matrix microreactors for the design of supramolecular complexes of proteins. Using ultracentrifugation analysis, it has been demonstrated that the oligomeric composition of various enzymes (ketoglutarate dehydrogenase, alkaline phosphatase, lactic dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase) solubilized in reversed micelles of Aerosol OT [sodium bis(2-ethylehexyl)sulfosuccinate] in octane changes upon variation of the degree of hydration. An oligomeric complex forms under conditions when the radius of the micelle inner cavity is big enough to incorporate this complex as a whole. At lower degrees of hydration the micelles ‘uncouple’ such complexes to their components. The catalytic properties of various oligomeric complexes have been studied. Possibilities of using reversed micelles for the separation of subunits of oligomeric enzymes under non-denaturating conditions have been demonstrated. In particular, the isolated subunits of alkaline phosphatase, lactic dehydrogenase and glyceralde-hyde-3-phosphate dehydrogenase have been found to be active in Aerosol OT reversed micelles. The dependences of the catalytic activity of oligomeric enzymes represent saw-like curves. The maxima of the catalytic activity observed at these curves relate to the functioning of various oligomeric forms of an enzyme. The radii of the micelle inner cavity under conditions when these maxima are observed correlate with the linear dimensions of the enzyme oligomeric forms. Correlation of the position of a maximum with the shape of an oligomeric complex is discussed.

Keywords: alkaline phosphatase/glyceraldehyde-3-phosphate dehydrogenase/ketoglutarate dehydrogenase/lactic dehydrogenase/reversed micelles

Received July 17, 1991;
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