LABORATORY OF MICELLAR ENZYMOLOGY

Head of the laboratory: Professor Andrey V.Levashov, Dr.Sc., PhD

Tel.: (7095) 939-3429, Fax: (7095) 939-0997, E-mail: levashov@mic.phys.msu.su

The main goal of the laboratory of micellar enzymology (it is now 10 years since the lab was announced) is studying the role of supramolecular organization of enzymes in their functioning. It was suggested for enzymes to be entrapped into surfactants aggregates, micelles, for modelling their natural biomembrane environment. Such aggregates can be formed in the systems surfactant-water-organic solvents. It is very easy to solubilize enzymes into micelles of different structure and sizes. Moreover, the level of the catalytic activity of enzymes can by easily regulated by micellar matrix, and can by much higher than that in water (in classical enzymology). Using the systems of reverse micelles the role of lipid and carbohydrate components in the enzyme regulation was studied. It is known that enzymes in Nature represent complex orginized glyco-lipo-protein assembles.

One of the laboratory tasks is to study the enzyme stability at different conditions (high temperature, organic solvents, etc.), and development of different approaches to stabilization of biocatalysts using surfactants, polymeric materials, polyelectolytes, etc.

About 200 papers were published since the laboratory exists, 50 specialists graduated from the laboratory (Faculty of Chemistry, Moscow State University), 30 PhD theses were successfully presented.

Publications:

1. N.L.Klyachko, A.V.Levashov, A.V.Kabanov, K.Martinek. Micellar enzymology: catalysis by enzymes entrapped into hydrated surfactant aggregates having various structures in organic solvents. In: Kinetics and Catalysis in Microheterogeneous Systems, M.Gratzel, K.Kalianasundaram, eds., Marcel Dekker Inc. 1991, p.135-181.

2. A.V.Levashov, A.V.Ugolnikova, M.V.Ivanov, N.L.Klyachko. Formation of homo- and heterooligomeric supramolecular structures by D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase in reversed micelles of Aerosol OT in octane. Biochem. Mol. Biol. Int. 1997, v.42, p.527-534.