Isolation and Characterization of Sunflower Protein Isolates and Sunflower Globulins

Abstract

Sunflower protein isolates and sunflower globulins were prepared from sunflower meals which were defatted by the method of aqueous enzymatic extraction and analyzed by gel filtration. The proximate composition, amino acid contents, functional properties of the proteins were investigated in present study. In addition, the proteins were also characterized by gel electrophoresis. The results showed that sunflower protein isolates contained less lysine than the FAO pattern of essential amino acid requirements while other amino acid levels were comparable. Functional properties of sunflower protein isolates were better or close to those of soybean protein isolates. Sunflower protein isolates showed three major fractions having molecular mass of 380×103, 100×103 and 27×103. 11S globulins were the major fraction of sunflower protein isolates. Chlorogenic acid was shown to be more associated with all proteins. It was found that there were 10 major bands in sunflower globulins with molecular mass ranging from 13000 to 53500, while sunflower protein isolates had more bands.