Flavor Protein Interactions: Characteristics of 2‐Nonanone Binding to Isolated Soy Protein Fractions

Abstract

ABSTRACTTHE ABSORPTION COEFFICIENTS at 280 nm of 1% solutions of pure soy protein, β‐conglycinin, glycinin, the acidic and basic sub‐units of glycinin were 6.04, 4.4, 8.04, 7.18, and 8.8, respectively. Using equilibrium dialysis the binding affinities of these proteins for the model flavor compound 2‐nonanone were determined. On an equivalent weight basis soy protein, β‐conglycinin and glycinin had approximately 5,2 and 3 primary binding sites per 100,000 daltons and affinity constants (K) of 570, 3050 and 540 m‐1, respectively, i.e., β‐conglycinin showed a fivefold greater affinity for nonanone than the other soy protein. The acidic and basic subunits showed binding behavior similar to that of glycinin.