Interactions of protein and starch studied through amyloglucosidase action

• Published in: Cereal chemistry 1997-11, Vol.74 (6), p.846-850
• Main Authors: Guerrieri, N, Eynard, L, Lavelli, V, Cerletti, P
• Format: Article
• Language: English
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; ALBUMINAS; ALBUMINE; ALBUMINS; ALMIDON; AMIDON; AMILOPECTINA; AMILOSA; AMYLOPECTIN; AMYLOPECTINE; AMYLOSE; BAKING; Biological and medical sciences; BLE; BLOOD PROTEINS; BREADMAKING; Cereal and baking product industries; COCCION AL HORNO; CUISSON AU FOUR; DEXTRINAS; DEXTRINE; DEXTRINS; DOUGHS; ENZYMIC ACTIVITY; Food industries; Fundamental and applied biological sciences. Psychology; GELATION; GELIFICACION; GELIFICATION; GLIADIN; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLUCOSA; GLUCOSE; GLUTEN; JELLIFICATION; MASA DE PANADERIA; MODELE; MODELOS; MOLECULAR WEIGHT; PANIFICACION; PANIFICATION; PATE DE CUISSON; PESO MOLECULAR; POIDS MOLECULAIRE; PROLAMINAS; PROLAMINE; PROLAMINES; PROTEINAS SANGUINEAS; PROTEINE SANGUINE; SERUM ALBUMIN; STARCH; STARCH GRANULES; TRIGO; WHEATS
• ISSN: 0009-0352; 1943-3638
• DOI: 10.1094/CCHEM.1997.74.6.846

The access of amyloglucosidase to the carbohydrate molecule was taken as a measure of interactions occurring among starch, amylose, amylopectin, beta-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