Fractionation and characterization of tartary buckwheat flour proteins

Protein fractions (albumin, globulin, prolamin and glutelin) were extracted from defatted tartary buckwheat flour. Albumin was the predominant protein fraction (43.8%) followed by glutelin (14.6%), prolamin (10.5%), and globulin (7.82%). Albumin was relatively rich in histidine, threonine, valine, phenylalanine, isoleucine, leucine and lysine. Globulin had high levels of methionine and lysine. Prolamin was high in histidine, threonine, valine, isoleucine, and leucine. Glutelin was rich in histidine, threonine, valine, isoleucine, and leucine. SDS–PAGE analysis, under non-reductive and reductive conditions, showed that disulfide bonds existed in the four fractions. Non-reduced albumin showed major bands at 64, 57, 41, and 38 kDa, and globulin at 57, 28, 23, 19 and 15 kDa. Reduced albumin and globulin shared two common bands at 41 and 38 kDa. Reduced prolamin showed major bands at 29, 26, 17 and 15 kDa. In vitro pepsin digestibility of the four fractions (from high to low) was: albumin > globulin > prolamin and glutelin.