RELATIONSHIP OF HYDROPHOBICITY AND SOLUBILITY WITH SOME FUNCTIONAL-PROPERTIES OF COWPEA (VIGNA-UNGUICULATA) PROTEIN ISOLATE

The relationship of hydrophobicity and solubility with some functional properties of cowpea protein isolate was determined. Cowpea protein isolate was prepared by alkali extraction followed by precipitation at pH 4.5. The precipitated proteins were then neutralized to pH 7. Heating of the protein isolate to 100-degrees-C for 10 min followed by cooling to room temperature resulted in a significant (P less-than-or-equal-to 0.05) decrease in aromatic hydrophobicity (ARH) when compared to the native protein isolate. The inclusion of sodium dodecyl sulfate (SDS) during heating gave a significant (P less-than-or-equal-to 0-05) 1.7-fold increase while inclusion of mercaptoethanol (ME) gave a significant (P less-than-or-equal-to 0.05) 2.5-fold increase in ARH of the cooled protein solution. Protein solubility (PS), foam expansion (FE) and emulsification activity index (EAI) of the isolate generally increased significantly (P less-than-or-equal-to 0.05) upon heating or treatment with urea or SDS or a combination of SDS and ME. Backward stepwise multiple regression was used to obtain equations for predicting emulsifying and foaming properties of the protein isolate from solubility and hydrophobicity parameters. PS, ARH and aliphatic hydrophobicity (ALH) were important in predicting foam stability and emulsion stability, while PS and ALH were important for predicting FE. ALH alone was important for predicting EAI.