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Berezin et al. (47,48) and Poon and Wells (50)are among the very few who used reverse micelles as media to investigate enzyme-catalyzed reactions at normal temperatures. Most of these reactions involve hydrolytic systems and their investigation under such conditions shows a complex relationship between enzyme activity and the various parameters influencing the micromicellar state. It is seen that reaction rates in the presence of reverse micelles are most often quite different from those observed in bulk water.

Another important parameter influencing the responses of a number of enzyme systems if the “polyanionic” microenvironment provided by the spherical monolayer of surfactants with anionic polar heads. We found that several hydrolytic enzymes, for example, trypsin hydrolysis of benzoyl-arginin ethyl ester are well accommodated at room temperature under selected conditions of medium but that the pHactivity profile of the tryptic hydrolysis of the substrate in micellar solutions is shifted compared to that obtained in bulk water (42).

I 350 400 450 500 550 600 A nm Fig. 19. 6 r M . The insert shows the variation of extinction coefficient of the Soret band as a function of H,O/ AOT ratios expressed in moles. CRYOENZYMOLOCY IN AQUEOUS MEDIA 43 An Aminco-Chance DW2 spectrophotometer, similarly equipped to investigate subzero temperatures, was used to carry out spectroscopic assays on solubilized enzymes, as well as to monitor enzyme-catalyzed reactions. T w o different apolar solvents were used, that is n-heptane and silicone oils of various molecular weight and viscosity, their freezing points being -90 and -5OoC, respectively.

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