L. Gajjar et al., ACTIVATION AND STABILIZATION OF ENZYMES ENTRAPPED INTO REVERSED MICELLES - STUDIES ON HYDROLYZING ENZYMES - PROTEASE AND ALPHA-AMYLASE, Applied biochemistry and biotechnology, 49(2), 1994, pp. 101-112
Observations of the activity of two hydrolyzing enzymes-protease and a
lpha-amylase-entrapped inside the reversed micelles formed by surfacta
nts in hexane, benzene, and cyclohexane are reported. The surfactants
chosen for this study are: Tween 80, a nonionic surfactant, Cetyl pyri
dinium chloride, a cationic surfactant, and two anionic surfactants, s
odium lauryl sulfate and Aerosol OT. Tween 80 enhances the activity of
both protease and alpha-amylase. Sodium lauryl sulfate and Aerosol OT
, which are ionic surfactants, enhance the activity of protease, but i
nhibit the activity of alpha-amylase. Cetyl pyridinium chloride, howev
er, enhances the activity of alpha-amylase, but inhibits the activity
of protease. Enhanced activity is generally severalfold greater in com
parison to the activity observed in the usual aqueous system in the ab
sence of reversed micelles. It has also been observed that the enhance
d activity of the enzymes entrapped inside the reversed micelles remai
ns preserved for a much longer period of time in comparison to the act
ivity in the,usual aqueous systems. These observations, which support
the view that with proper choice of surfactant and the organic solvent
, reversed micelles act like a microreactor that provides a favorable
aqueous microenvironment for enzyme activity, have biotechnological ov
ertones.