Studies on the specificity of a lipase system fromGeotrichum candidum.

The lipase system fromGeotrichum candidum preferentially hydrolyzed oleic acid, regardless of position, from the four possible racemic triglycerides containing oleate and palmitate. The rate of hydrolysis of these glycerides was most rapid when the substrate contained two moles of oleate. This acid was also preferentially released from a series of triglycerides containing oleate and two moles of a saturated fatty acid. The chain length of the latter did not alter the specificity for oleate.Equimolar quantities of oleic and linoleic acids were released when triolein and trilinolein (equimolar mixture) were hydrolyzed by this lipase. No differentiation between oleate and palmitoleate was observed when racemic glyceryl 1-palmitoleate-2,3-dioleate was the substrate. However, only 7.2 M%cis-vaccenic acid was released from glyceryl 1-cis-vaccenate-2,3-dioleate and 5.4 M% petroselinic acid from glyceryl 1-palmitoleate-2,3-dipetroselinate. It therefore appears that the enzyme may be specific forcis-9-unsaturation as well as forcis-9,cis-12-unsaturation. When specificity was assumed, the fatty acid compositions of the diglycerides obtained from digestions withG. candidum were close to theoretical.