Chia ( Salvia hispanica L.) is a plant that produces seeds rich in some nutraceutical compounds with high protein content, but little is known about them; for this reason the aim of this study was to characterize the seed storage proteins. Protein fractions were extracted from chia seed flour. The main protein fraction corresponded to globulins (52%). Sedimentation coefficient studies showed that the globulin fraction contains mostly 11S and 7S proteins. The molecular sizes of all the reduced fractions were about 15-50 kDa. Electrophoretic experiments under native conditions exhibited four bands of globulins in the range of 104-628 kDa. The denaturation temperatures of crude albumins, globulins, prolamins, and glutelins were 103, 105, 85.6, and 91 °C, respectively; albumins and globulins had relatively good thermal stability. Selected globulin peptides by mass spectrometry showed homology to sesame proteins. A good balance of essential amino acids was found in the seed flour and globulins, especially of methionine+cysteine.
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