I. Andriot et al., Interactions between methyl ketones and beta-lactoglobulin: Sensory analysis, headspace analysis, and mathematical modeling, J AGR FOOD, 48(9), 2000, pp. 4246-4251
Interaction of flavor compounds with proteins is known to have an influence
on the release of flavor from food. Hydrophobic interactions were found be
tween beta-lactoglobulin and methyl ketones; the affinity constant increase
s by increasing the hydrophobic chain. Addition of beta-lactoglobulin (0.5
and 1%) to aroma solutions (12.5, 50, and 100 mu L L-1) of three methyl ket
ones induces a significant decrease in odor intensity. The chosen methyl ke
tones were 2-heptanone (K-b = 330), 2-octanone (K-b = 950), and 2-nonanone
(K-b = 2440). The release of these flavor compounds (50 mu L L-1) was studi
ed by static headspace in water solution (50 mM NaCl, pH 3) with different
concentrations of beta-lactoglobulin (0, 0.5, 1, 2, 3, and 4%). Increasing
the concentration of protein increases the retention of volatiles, and this
effect is greatest for 2-nonanone, the compound with the highest affinity
constant, and lowest for 2-heptanone. A mathematical model previously devel
oped to describe flavor release from aqueous solutions containing flavor-bi
nding polymers (Harrison, M.; Hills, B.P. J. Agric. Food Chem. 1997, 45, 18
83-1890) was used to interpret the data. The model assumes that the polymer
-flavor interaction is reversible and the rate-limiting step for release is
the transfer of volatiles across the macroscopic gas-liquid interface. Thi
s model was used to predict the equilibrium partitioning properties and the
rate of release of the three methyl ketones. Increasing the affinity const
ant leads to decreased release rates and a lower final headspace aroma conc
entration.