Interactions between tannins and proteins isolated from broad bean seeds (Vicia faba Major) yield soluble and non-soluble complexes

Abstract

The binding of tannin fraction to protein fractions isolated from broad bean seeds was studied by precipitating potential and fluorescence quenching methods. The tannin fraction with high proanthocyanidins content was isolated from broad bean coats. Storage proteins of broad bean, 11S, 7S, and 2S, were isolated from broad bean cotyledons and purified. Gelatin, BSA, as well as broad bean 2S and 7S protein fractions exhibited similar shape of curves illustrating the effect of pH on protein precipitation and were precipitated by broad bean tannin fraction over the wide range of pH. For pea proteins isolate and 11S fraction of broad bean proteins, quite different effect of pH was observed. The relationships between the amount of protein–polyphenols complex precipitated and the content of tannin fraction were linear and characterized by high squared correlation coefficients ranging from 0.9613 to 0.9938. Among the protein fractions isolated from broad bean seeds, the highest precipitating potential was noted for 11S fraction, followed by 7S and 2S fractions and amounted to 1.63, 1.34, and 0.87, respectively. To characterize the association of proteins with phenolic compounds yielding formation of soluble complexes, fluorescence spectroscopy was applied. Similarly, the most extensive fluorescence quenching was observed in the case of 11S protein fraction.