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ABSTRACT

Binding of vanillin by fababean protein micellar mass (PMM) in water suspensions was investigated. Free vanillin was determined by HPLC and data were evaluated by the Klotz equation. Increasing vanillin and PMM concentrations increased the percentage of total vanillin bound to protein. Binding capacities of heat-treated (denatured) PMM were higher than that of untreated (native) PMM. Binding forces between vanillin and PMM were weak, and the number of binding sites increased when PMM was denatured.