Exocellular phospholipase C activity from a Propionibacterium acnes strain isolated from a periodontal pocket

The culture supernatant of a strain of Propionibacterium acnes was investigated for its phospholipase (PL) activity. The microorganism was isolated from a periodontal pocket of a patient with periodontal disease. Supernatants from cultures of this microorganism were used as a source to obtain enzymes. Proteins from the supernatants were concentrated, and their enzymatic activity was partially purified through molecular sieving. The procedure yielded two peaks of activity. This activity was shown to hydrolyze phosphatidyl choline (PC) and phosphatidyl ethanolamine (PE) and was effective in a pH range of 5 to 9, with an optimal activity at pH 7.0. Divalent cations were not required for activity of the enzymes. Analysis of the products obtained from the hydrolysis of PC labeled in the choline, phosphoryl, or acyl moieties and PE containing labeled oleic acid indicated that the supernatants' activity was mostly phospholipase C (PL-C). Phospholipase C can act synergistically with other factors to produce tissue damage, and hence may contribute to the pathogenesis of periodontal disease.