Abstract
Bacteroides gingivalis (both W 83 and ATCC 33277 strains), B. asaccharolyticus (ATCC 25260), and B. melaninogenicus (ATCC 25845) produced hydrolytic activity on the synthetic peptide 4-phenylazobenzyl-oxycarbonyl-L-prolyl-L-leucyl-glycyl-prolyl-D-arginine (PZ peptide) during their early logarithmic phase of growth. The PZ-peptidase activity of the ATCC 25260 strain was the highest with an initial rate of reaction at 0.54 nmol PZ-pro-leu/h per 108 cells. Relatively low levels of PZ peptidase were produced by the pathogenic W 83 cells. In all the strains tested, no further increase in PZ-peptidase activity was detected after the late logarithmic phase, even when the cultures lysed. The result of the protease test seems to indicate that the PZ-peptidase activity of both oral strains of B. gingivalis is collagenase, while that of B. asaccharolyticus may be a mixture of protease and collagenase enzymes.
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