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Volume 44, Issue 6

Effect of mucin and glucose on proteolytic and glycosidic activities of No Access

Abstract

The production of glycosidase and protease activities, which may play a role in the degradation of human glycoproteins, by strains isolated from endocarditis, septicaemia or the oral cavity was investigated with a range of fluorogenic substrates. The pH optima of the proteases ranged from 6.0 to 9.3 and the pH optima for the glycosidases were lower (4.5-6.0), although the pH range over which both groups of enzymes acted was broad. Growth in a minimal medium supplemented with glucose resulted in repression of glycosidase activities and elevated proteolytic activity. Bacteria from cultures supplemented with porcine gastric mucin (PGM), a model glycoprotein, exhibited higher levels of glycosidase activity, while proteolytic activity was suppressed and glycoprotein-derived monosaccharides were transported at significantly higher rates than those observed for cells grown in media with glucose. PGM-derived cells also exhibited high levels of N-acetylneuraminate pyruvate-lyase, the first intracellular enzyme in the pathway of sialic acid catabolism. Taken together, these data indicate that strains produce a range of proteolytic and glycosidic enzymes that may play a role in the degradation of host-derived glycoproteins.

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© J. MED. MICROBIOL. 1996
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1996-06-01
2025-11-16

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/content/journal/jmm/10.1099/00222615-44-6-409
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Effect of mucin and glucose on proteolytic and glycosidic activities of Streptococcus oralis
J. Med. Microbiol. 44, 409 (1996); https://doi.org/10.1099/00222615-44-6-409
/content/journal/jmm/10.1099/00222615-44-6-409
/content/journal/jmm/10.1099/00222615-44-6-409
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