Summary: All of eight Mycoplasma strains tested were capable of hydrolysing tributyrin. The saprophytic strains showed the lowest lipolytic activity, and the parasitic the highest. The properties of lipase were studied in some detail. The lipolytic activity of this organism was highest at the logarithmic phase of growth and declined steeply afterwards. The enzyme was not bound to the cell membrane and appeared in the soluble fraction of disrupted cells. The cell extract hydrolysed tributyrin much faster than trilaurin or triolein. Methyl oleate and ‘Tween 80’ were only slowly hydrolysed. Cholesteryl acetate and stearate were not hydrolysed by cell extract or by intact . Partial purification of the lipase was accomplished by ammonium sulphate fractionation of cell-extract proteins, followed by anion-exchange chromatography. The partially purified enzyme did not require inorganic ions for activity and its optimal pH value varied between 7·5 and 8·0, depending on the substrate tested.


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