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ABSTRACT

The solubilities of teparies albumin (TA) and globulin (TG) compared to soy protein isolate (SPI) were higher at pH 1–4 but similar at pH 8–12. Although SPI developed significantly higher viscosity than the tepary bean proteins, the flour (TF) and TA had significantly higher heat coagulability and foaming properties. TG did not coagulate upon heating (100°C). Also, TG formed a weaker and less stable foam and had significantly lower emulsion capacity than TF, TA, and SPI. Tepary bean proteins absorbed significantly higher amounts of fat (corn oil) than SPI.