Characteristics of the lipase from the mold,Geotrichum candidum: A review

The moldGeotrichum candidum produces an extracellular lipase, readily concentrated by removal of the culture medium in which the microorganism is grown. The lipase is characterized by a unique, but not absolute, specificity for fatty acids containingcis-9 orcis,cis-9, 12 unsaturation, hydrolyzing both regardless of position within the triglyceride molecule. The enzyme also hydrolyzescis-9-16∶1,cis,trans-9,12-18∶2,trans,cis-9,12-18∶2, palmitoyl oleate and cholesteryl oleate. Digested at comparatively slow rates are:trans,trans-9,12-18∶2, double bond positional isomers of 18∶1 (other thancis-9), stearolic acid, oleoylpalmitate, dilinoleoyl phosphatidyl choline, and saturated acids. The enzyme has an optimum pH of 8.2, and the lyophilized powder is extremely stable, retaining activity for at least eight years when stored at-20 C. A purification of 81-fold has been achieved. One of five papers presented in the Symposium “Microbial Lipolytic Enzymes,” AOCS Spring Meeting, New Orleans, April 1973. Scientific contribution 556, Agricultural Experiment Station, University of Connecticut, Storrs, Conn. 06268.