The peptide hydrolase system of Bifidobacterium infantis, B. longum an
d B. adolescentis revealed the presence of aminopeptidase, dipeptidase
, tripeptidase, carboxypeptidase and caseinolytic activity. A rather s
pecific trypsin-like activity hydrolyzing benzoyl arginine P-nitroanil
ide was also detected in the 3 species of Bifidobacterium. PAGE electr
ophoresis revealed the presence of one aminopeptidase and two dipeptid
ases in each of the strains tested.