SUMMARY: strain 5, an anaerobic rumen bacterium, produced an extracellular lipase during exponential growth in batch cultures. The lipolytic activity was excluded from Sephadex G-200, and the purest preparations obtained contained two components when examined by electrophoresis or by ultracentrifugation and a large proportion of nucleic acid. The enzyme was most active at pH 7.4 and at 20 to 22°; activity was enhanced by Cal or BaCl while ZnCl and HgCl were inhibitory. Sodium chloride at high concentration was also inhibitory. Trilaurin was most rapidly hydrolysed of the triglycerides but diglycerides were more rapidly hydrolysed than were triglycerides.


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