Abstract
Protein extractability studies showed that the protein of broad bean ( Vicia faba L.) was extractable at both acidic and basic pH. The percentage of pH-12 extractable protein that was precipitated at pH 4 (isoelectric point) from protein concentrate, dehulled full-fat seed flour and whole seed flour are 62.0%, 61.2% and 71.6%, respectively. Low ionic strength (μ⩽0.4) increased the solubility of the protein in the bean concentrate at acidic pH, while at alkaline pH, increase in ionic strength (0.1–2.0) had an inverse relationship on the concentrate protein solubility. The capacity to form protein-stabilized foam was least (34%) at pH 4 and highest (97%) at pH 12. These were increased to 62% (pH 4) and 139% (pH 12) in medium with ionic strengths of 0.2 and 0.4, respectively. The foam formed was more stable at pH 4 than at the other pHs. Low ionic strength of 0.1 improved water absorption capacity but reduced it at ionic strength of ⩾0.6.
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