Functional Properties of the Great Northern Bean (Phaseolus vulgarisL.) Proteins: Sorption, Buffer, Ultraviolet, Dielectric, and Adhesive Properties

摘要

ABSTRACTSeveral functional properties of the Great Northern bean (Phuseolus vulgurisL.) proteins were investigated. Sorption isotherms of the bean flour, albumins, globulins, protein concentrates, and protein isolates had similar patterns at corresponding temperatures. The bean flour registered higher equilibrium moisture content than albumins, globulins, protein concentrates, and protein isolates at corresponding temperature and equilibrium relative humidity. Buffer capacity of the bean proteins in the pH range 4–8 was modest. Modification (succinylation and oxidation) improved oil absorption capacity of the bean proteins. Water absorption capacity of the bean flour and protein isolates increased on modification. Modification of the bean proteins decreased the yellowness and increased the redness. About 1–2 KV/mm thickness potential difference was necessary for the passage of electrical current through these proteins. Globulins registered the highest stickiness (92N) among the samples investiga