Oat lipase

Abstract

The lipase causing lipolysis in oatmeals was shown to be a true cereal lipase, not a product of the subepidermal fungal contaminants. This lipase was purified some 2000 fold on a dry-matter basis compared with the activity in the original oatmeal. The purified prepn. contained 6.7% N and 0.5% P. The purified prepn. has an opt. pH of 7.4, opt. temp. 37-38[degree], and a Michaelis-Menten constant (Km) of 0.006[image] when tributyrin is the substrate. The purified lipase splits off one butyric acid radical only from tributyrin and does not hydrolyze the various mono-and di-butyrins at pH 7.4 and 37[degree]. The oat lipase will not attack the polyoxyethylene derivative of sorbitan laurate nor is it "activated" by the compensatory activators required, according to Willstatter, by pancreatic lipase.