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Interactions of Protein and Starch Studied Through Amyloglucosidase Action

November 1997 Volume 74 Number 6
Pages 846 — 850
Nicoletta Guerrieri , 1 Lucia Eynard , Vera Lavelli , and Paolo Cerletti

DISMA Dipartimento di Scienze Molecolari Agroalimentari and CISMI Centro Interuniversitario Studio Macromolecole Informazionali, Via Celoria 2, 20133 Milano, Italy


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Accepted July 4, 1997.
ABSTRACT

The access of amyloglucosidase to the carbohydrate molecule was taken as a measure of interactions occurring among starch, amylose, amylopectin, β-dextrin and purified gluten, gliadins, high molecular weight glutenin subunits, or bovine serum albumin when they were mixed together and gelatinized before digestion. The most relevant decrease in liberated glucose, denoting coverage of some reaction sites for amyloglucosidase, occurred when gliadins were mixed with the carbohydrates. Other proteins were not as effective as gliadins. Amylopectin was not affected by any protein. Comparison of results allows some hypothesis to be formulated about the influence of structure on molecular interactions.



© 1997 by the American Association of Cereal Chemists, Inc.