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Phospholipase A activity in supernatants from cultures of Bacteroides melaninogenicus

1981; Elsevier BV; Volume: 664; Issue: 1 Linguagem: Inglês

10.1016/0005-2760(81)90037-0

1879-145X

Jaime Bulkacz, J. Erbland, John MacGregor,

Biochemical Analysis and Sensing Techniques

The phospholipase A activity in culture supernatants of two strains of Bacteroides melaninogenicus is described. The enzymes utilize phosphatidylcholine as substrate and produce mainly lysophosphatidylcholine and free fatty acids. The activities are Ca2+-independent, are not affected by the presence of a chelating agent, have a broad pH range (5–9) and an optimum temperature for activity of approx. 50°C. The activity in a growing bacterial culture increases from the end of the lag phase to the late exponential phase of growth. Analysis of the products resulting from the actions of the enzymes on L-α-palmitoyl-β-oleoyl [1-14C]phosphatidylcholine indicates that the enzymes are phospholipase A1 (EC 3.1.1.32).