An enhancement in the activity of papain (EC 3.4.22.2) was described in mix
ed reverse micellar systems containing Tween80 compared with those without
Tween80. By the use of these media, the hydrolytic and synthesis activities
of papain were investigated in detail, respectively for the hydrolysis of
N-alpha -benzoyl-L-arginine-p-nitroaniline (BNPNA) and the synthesis of the
dipeptide Z-Gly-L-PheOMe (ZGPM). The reaction medium conditions (W-0, pH a
nd Tween80 concentration) were optimized for both the hydrolytic and synthe
sis reactions. The results showed a pronounced increase in the papain activ
ity when a moderate amount of Tween80 was added into sodium di-2-ethylhexyl
sulfosuccinate (AOT) or tetradecyltrimethylammonium bromide (TTAB) reverse
micelles, either in the yield of dipeptide synthesis or in the initial rate
of BNPNA hydrolysis. In addition, a mechanism to explain the enhancement o
f enzymatic activity was proposed according to the change of the optimal pa
rameters in the mixed and non-mixed reverse micellar systems, which is asso
ciated with the environmental polarity surrounding the solubilised enzyme m
olecules. (C) 2001 Society of Chemical Industry.