Cereal Chem 43:644 - 657.  |  VIEW ARTICLE

The Glycerol Ester Hydrolases of Wheat Germ.

C. E. Stauffer and R. L. Glass. Copyright 1966 by the American Association of Cereal Chemists, Inc. 

The presence in aqueous extracts of wheat germ of three distinct esterolytic enzyme activities has been established. One, on esterase, hydrolyzes aqueous solutions of esters, and is most active toward triacetin. A second, termed a tributyrinase, hydrolyzes emulsions of esters but appears to be less active toward esters in solution. It is most active with tributyrin as a substrate. A third enzyme, a lipase, will catalyze the hydrolysis of emulsified mono-olein. Data on the enzymatic and proteinaceous characteristics of these three enzymes are presented to characterize their differences.