A lipases (glycerol ester hydrolases E. C. 3.1.1.3) from a brazilian s
train of Penicillium citrinum has been investigated. When the microorg
anism was cultured in the simple medium (1.0% olive oil and 0.5% yeast
extract), using olive oil in as carbon source in the inocula, the enz
yme extracted showed maximum activity (409 IU/mL). In addition, decrea
se of yeast extract concentration also reduces the lipase activity. Ne
vertheless, when yeast extract was replaced by ammonium sulfate, no ac
tivity was detected. Purification by precipitation with ammonium sulfa
te showed best activity in the 40-60% fraction. The optimum temperatur
e for enzyme activity was found in the range of 34-37 degrees C. Howev
er, after 30 min at 60 degrees C, the enzyme was completely inactivate
d. The enzyme showed optimum at pH 8.0. The dried concentrated fractio
n (after dialysis and lyophilization) maintained its lipase activity a
t room temperature (28 degrees C) for 8 mo. This result in lipase stab
ility suggests an application of lipases from P. citrinum in detergent
s and other products that require a high stability at room temperature
.