Laboratory findings demonstrate high phospholipase C activity in Pseudomonas fluorescens, suggesting important enzymatic roles.
A strain of Ps. fluorescens which secretes phospholipase C into a culture medium was accidentally found in our laboratory. The correlation between the growth of bacteria and phospholipase C production was studied and the increase of the activity in the growth medium was observed up to 96 h. The enzyme preparation partially purified with ammonium sulfate precipitation, showed high phospholipase C activity, i. e. most of lecithin was converted to diglyderide. The activity was optimum at pH 5.0. Michaelis constant was 44μM and maximal velocity was 250n moles/mg protein/h.
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Masaru et al. (1973) studied this question.
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