Proteolytic activity and degradation of alpha(s1)- and beta-casein wer
e tested with 5 strains of Brevibacterium linens. The highest proteoly
tic volume activity was found in the culture supernatant of strain DSM
20426. The proteolytic specific activity of the supernatants of the t
ested strains ranged from 3 to 22 mg casein degraded/h . protein. Two
strains were able to degrade both, alpha(s1)- and beta-casein complete
ly, whereas the other strains preferred beta-casein. Corresponding to
the differences in degradation kinetics, different degradation product
s were found in electrophoretic patterns.