Protein-protein interactions in reverse micelles: trypsin shows superactivity towards a protein substrate alpha-chymotrypsinogen A in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT) in isooctane.

Protein-protein interactions in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT), in isooctane containing varying amounts of Tris buffer are studied by using activation of alpha-chymotrypsinogen A by trypsin (EC 3.4.21.4) to alpha-chymotrypsin (EC 3.4.21.1) as a model reaction. It has been found that protein-protein interactions are strongly dependent on the water content of the medium. At an optimum water content the activation reaction in reverse micelles is faster than reaction in water by a factor of 21.3. At lower water content both reaction rates and the conversion of alpha-chymotrypsinogen A into alpha-chymotrypsin decrease with decrease in water content of the reaction medium.