The enzymetic activity of RNaseA solubilized in reverse micelles formed in cyclohexane by dodecylammonium butyrate(DAB) and water has been investigated with the use of cytidine 2’, 3’-phosphate as the substrate. In the investigated concentration range, RNaseA exhibited a "superactivity" in the DAB reverse micelle.
The activity and conformation of ribonuclerse A (RNaseA) solubilized in cyclohexane via dodecylammonium butyrate(DAB) reverse Ancelles were investigated. The activity of RNaseA was studied using the cytidine 2’,3’-phosphate as the substrate, and it was found that kcat increases significantly with respect to that in water attended by an increased Km·FT-IR spectra of RNaseA in reverse Ancellax solution were investigated as a function of w0(= [H2O]/ [DAB]), and it was noted that the structure of RNaseA became looser in reverse micelles campared to that in aqueous solution. The relation between activity and conformation was discussed.
