Binding of aroma compounds with legumin. III. Thermodynamics of competitive binding of aroma compounds with 11S globulin depending on the structure of aroma compounds

This paper considers the prominent features in competitive binding of aroma esters from their mixtures to 11S globulin of broad beans (legumin) in aqueous medium at pH 7.2 and ionic strength of 0.05 mol dm⁻³. Series of alkyl acetates (C₄–C₈) and methyl esters of carbonic acids (C₅–C₉), differing in the length of hydrocarbon chain, have been under our studying. To accomplish the ends of the study, a combination of ultrafiltration and gas–liquid chromatography (GC) has been used. An increase in the length of hydrocarbon chain of the aroma esters brought about greater binding affinity for the protein, the occurrence of some structural restrictions in the interior of the protein molecule, preventing binding, and the change in the binding mechanism of the aroma compounds at the specific critical length of hydrocarbon chain. Differential scanning microcalorimetry data suggested that the revealed changes in the binding mechanism of the studied aroma compounds were attributable to the conformational modification of the protein globule as a result of binding with the aroma compounds. A distinguishing feature in binding of methyl esters of carbonic acids with legumin was their greater binding affinity for the protein as compared with alkyl acetates. The mutual effect of aroma compounds on binding from their equimolar mixtures to the protein made itself evident, firstly, as a drastic increase in the binding extent of aroma esters, having rather long hydrocarbon chain and, secondly, as a dramatic change in the binding mechanism of the aroma esters with relatively short hydrocarbon chain.