The 7S and 11S proteins were extracted from six representative soybean varieties. The purities of 7S and 11S proteins which were purified by the Superdex 200 gel column chromatography and validated by SDS-PAGE and protein purification device gel column chromatography were more than 90%. The correlation between amino acid composition and surface hydrophobicity of 7S and 11S proteins was studied. The results showed that the surface hydrophobicity of 7S and 11S proteins was positively correlated with the contents of Gly, Cys, Pro, Ala, Val, Met, Tyr, Asp, Thr and His, while it had negative correlation with the contents of Ile, Leu, Phe, Ser and Lys, and it was not related with the contents of Glu and Arg. It was indicated that the content of hydrophobic amino acids was positively correlated with the surface hydrophobicity of 7S and 11S proteins, while the content of hydrophilic amino acids was not associated with its surface hydrophobicity. |