SUMMARY: A Penicillium roqueforti strain produced maximal amounts of lipase when grown in 0.5% casitone‐1% Proflo broth, pH 5.5, at 27°C. Addition of butteroil, com oil or olive oil to the growth medium inhibited the lipase production. Under pH stasis the partially purified lipase of P. roqueforti had an optimum pH of 8.0 and an optimum temperature of 37°C. Maximum lipolytic activity occurred with 5% butteroil emulsion as the substrate. Manganese chloride and magnesium chloride stimulated the enzyme activity. Calcium, sodium and potassium sale had no appreciable effect on lipolysis; silver, mercury and zinc salts were inhibitory. The lipase was thermolabile, being inactivated completely within 10 min at 50°C. The lipase hydrolyzed tributyrin, tricaprylin, tricaprin, tripropionin and triolein in decreasing order.

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