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BSTRACT: Protein isolate (PI) was prepared from 3 cowpea varieties and 2 soybean varieties in each of 2 y. The protein contents of cowpea PI (CPI) (91.4% to 91.8%) and soy PI (SPI) (93.0% to 93.5%) were significantly different ( P < 0.05). Electrophoretogram showed that CPI was concentrated at 60 and 40 kDa, whereas SPI showed bands at 95, 65, 60, 40, and 35 kDa. The CPI had higher lysine (49.3 to 51.8 mg/g) than SPI (41.9 to 43.4 mg/g). The CPI and SPI had surface hydrophobicities ranging from 387.8 to 572.9 and 640.6 to 643.1, respectively. Denaturation temperature (85.2 to 88.4 °C) and enthalpy (8.42 to 10.33 J/g) of CPI were similar to the 7S fraction of SPI (82.6 °C and 96.0 to 96.3 J/g). These characteristics of CPI might be useful to explain its functionalities for application in food systems. [ABSTRACT FROM AUTHOR]

BSTRACT: Functional properties of protein isolates prepared from 3 cowpea varieties and 2 soybean varieties in each of 2 y were determined. Both cowpea protein isolate (CPI) and soy protein isolate (SPI) showed a u-shaped curve for solubility with the minimum solubility occurring at pH 4.5. The CPI had lower emulsifying activity than SPI but was similar in stability. Foaming capacity and foaming stability ranged from 58.6 to 60.2 mL and 63.7 to 64.4 min for CPI and from 31.9 to 33.0 mL and 43.4 to 45.0 min for SPI, respectively. Gels were formed at 70 °C for 40 min and 30 min for CPI (12%) and SPI (10%), respectively. The CPI needs modification to enhance functional properties for potential application in food products. [ABSTRACT FROM AUTHOR]