Ai. Pintado et al., Caseinolytic activity of fruit extract from Opuntia ficus-indica on bovine, caprine, and ovine sodium caseinates, BIOTECH PR, 17(4), 2001, pp. 643-646
The rates and extents of hydrolysis of alphas- and beta -caseins from bovin
e, caprine, and ovine sodium caseinates produced by an enzymatic extract of
the fruit of Opuntia ficusindica, (L.) Miller were evaluated and compared
with those produced by a commercial animal rennet. A mechanistic model base
d on a pseudo-first-order enzymatic reaction, in the presence of first-orde
r deactivation of the enzyme, was postulated and successfully fitted to the
experimental data. The animal rennet exhibited higher enzymatic efficiency
than the fruit extract, irrespective of the source (i.e., bovine, caprine,
or ovine) and the type (i.e., alphas- or beta -casein) of substrate. The e
nzymatic efficiency (k(cat)/K-m) for alphas-casein ranged from 72 to 220 an
d from 43 to 65 L g(-1) h(-1), and for beta -casein from 242 to 742 and fro
m 55 to 164 L g(-1) h(-1), for the animal rennet and the enzymatic extract
of O. ficus-indica, respectively. Finally, it was observed that beta -casei
n from caprine and ovine caseinates was degraded by O. ficus-indica faster
than its alpha (S) counterpart, but the reverse was observed for bovine cas
einate.