RESUMEN
The chemical compositions, intermolecular interactions, and functional properties of guar germ proteins (GGP) were investigated at different extraction pH (7 to 11). The protein efficiency ratio, essential amino acid index (46.53), predicted biological value (39.02), nutritional index (42.67), and protein purity (91.69 %) were found to be highest at pH 9. The in-vitro protein digestibility of GGP sample was highest at pH 11. From SDS-PAGE, the band intensity (<10 kDa) became thinner with an increase in extraction pH from 7 to 9 and then thicker. Meanwhile, smallest particle size and weaker ionic and hydrogen bonds were found at pH 11. The ß-sheet content was more dominating in GGP samples. Moreover, higher denaturation temperatures of GGP samples indicated that protein molecules had a compact tertiary structure. Furthermore, the GGP extracted at pH 7 showed better functional properties. The principal component analysis suggested that pH 9 was more suitable for isolating GGP.