Functional properties of native and succinylated lentil (Lens culinaris) globulins

The functional properties of native and succinylated lentil globulins were evaluated. Succinylation caused a shift in the isoelectric pH of native globulins from 4.5 to 3.5 and improved the solubility above pH 4.0. However, below this pH the solubility of succinylated globulins was reduced. The water absorption and the viscosity of the sucinylated globulins were increased by almost 100%, while there was a decrease in the oil absorption capacity. The extent of succinylation used in this study did not show any significant relationships to these functional properties. Emulsion activity was also increased by succinylation; being 54.1% for the native globulins, 60% for the 57.9% succinylated globulins and 62.7% for the 87.2% succinylated globulins. Similarly, the emulsion stability was also improved. Foaming capacity of the succinylated globulins was decreased slightly, while foam stability, except at pH 2.5, was considerably reduced. Native and succinylated globulins showed maximum foam stabilities at pH 3.5 and 2.5, respectively.