Publication no. C-2002-0802-07R |  VIEW ARTICLE

Esterases in Barley and Malt.

Robert E. Ward (1) and Charles W. Bamforth (1,2). (1) Dept. Food Science & Technology, University of California, Davis, CA 95616. (2) Corresponding author. E-mail: <cwbamforth@ucdavis.edu> Phone: 530-752-1467. Fax: 530-752-4759. Cereal Chem. 79(5):681-686. Accepted April 9, 2002. Copyright 2002 American Association of Cereal Chemists, Inc.

Several esterases from barley and malt have been separated on polyacrylamide gels. The slowest moving bands appear to represent a single enzyme displaying a spread of migration owing to differences in surface charge. During malting, this enzyme, which is located in the starchy endosperm, shifts to a more migratory form. Two other main esterase groups are identified through gel electrophoresis, notably a highly anionic, highly labile enzyme, MW 62,000, located in the aleurone. The slowest and fastest moving bands have been partially purified using salt fractionation and ion-exchange chromatography. The former, MW 47,000, has strong capability for hydrolyzing acetylxylan and it is speculated that its role in the starchy endosperm is as part of the enzyme system that hydrolyzes the cell walls.