Positional Specificity and Stereoselectivity of a Lipase Preparation from Oat Seeds Acting on 1, 2, 3-Trihexanoylglycerol

Abstract

Oat seed lipase was extracted with 0.01 M calcium chloride solution containing 0.5% Triton X-100 and precipitated with ammonium sulfate. The precipitate was dissolved in phosphate buffer at pH 6.0 and the supernatant was used as the lipase preparation. The lipase was very selective in the ester positions of 1, 2, 3-trihexanoylglycerol, hydrolyzing sn-3 most quickly, sn-1 moderately, and sn-2 hardly at all.