Reverse micelles are formed in apolar solvents with synthetic detergents or natural surfactants, with or without a cosurfactant (Luisi et al., 1988, Schelly (1997). It is visualized that the water-soluble enzymes arrange themselves in the internal water space of the micelle. In addition to soluble and membrane proteins, reverse micellar systems are able to house nucleic acids, plasmids, organelles and even various types of cells (Chhabra et al., 1997; Tuena de Gómez-Puyou and Gómez-Puyou, 1998). Most enzymatic studies have been performed using reverse micelles formed from well-characterized synthetic surfactants. However, these molecules are generally toxic and can not be used in potential pharmaceutical applications of enzymes contained in reverse micelles. Lipids such as lecithin are an attractive alternative to form reverse micelles. Furthermore, these phospholipid (PL)-reverse micelles can be used as model systems that simulate biological membrane (Darszon and Shoshani, 1992).

We have found that photosynthetic complexes of purple bacteria (Rhodospirillum rubrum) can be functionally transferred into reverse micelles, fabricated with natural emulsifiers, phospholipids (mainly phosphatidylcholine) (Srivastava et al., 2001). In this paper we have shown that these bacterial photosynthetic complexes (BPCs) can be innnobilized in a commercially available resin, araldite, and could be preserved active at room temperature for several months. We have explored the effects of temperature on the photosynthetic activity of the BPCs in reverse micelles. Bacterial chlorophyll (BChl) fluorescence induction kinetics (Strasser and Ghosh, 1995) and photo-oxidation of P (Woodbury anl Allen, 1995) were used as tools to measure the photosynthetic activity of BPCs.