The antimutagenic potential of casein was investigated using several m
utagens, including some food-related mutagens, and the Salmonella/micr
osome and Escherichia coli DNA-repair tests. The effect depended on th
e type of mutagen and the incubation time of casein with the mutagens.
Casein was very effective against benzo[a]pyrene, N-methylnitrosourea
and nitrosated 4-chloroindole, and was less effective towards sodium
azide and N-nitroquinoline-1-oxide (NQO). Preincubation increased the
antimutagenic potential of casein towards NQO. Heating of casein (up t
o 20 min at 130-degrees-C) did not alter its antimutagenic capacity. T
he effect of pepsin hydrolysis under simulated gastric conditions on t
he antimutagenic capacity of casein was tested with sodium azide and N
QO in the Salmonella/microsome test. The peptides formed were separate
d by ultrafiltration or by isoelectric precipitation of casein, and we
re characterized by HPLC size-exclusion and Kjeldahl analysis. The ant
imutagenic potential of casein increased with pepsin hydrolysis; this
increase was due to the peptides formed and might be explained by a be
tter accessibility of casein peptides for interaction with mutagens. T
he antimutagenic potential of pepsin-hydrolysed casein towards sodium
azide was observed over the whole dose-response curve.