In a previous communication (Langmuir 1997, 13, 6980-6984) we reported
stabilization of water-in-CO2 (wic) microemulsions by fluorinated dic
hained sulfosuccinate surfactant 'di-HCF4'. In this paper we present a
study of enzyme-catalyzed reactions affected in this w/c microemulsio
n in which the enzyme is located within the dispersed water droplets.
Two reactions, a lipase-catalyzed hydrolysis of p-nitrophenol butyrate
and lipoxygenase-catalyzed peroxidation of linoleic acid were examine
d. The activity of both the enzymes in the w/c microemulsion environme
nt were essentially equivalent to that in a water-in-heptane microemul
sion stabilized by Aerosol OT, a surfactant with the same headgroup as
di-HCF4. The inherent condition of low pH of the water droplets in th
e w/c microemulsion was improved using the buffer MES [2-(N-morpholino
)ethanesulfonic acid] which was shown to fix the pH in the range 5-6 d
epending on buffer concentration, pressure, and temperature.