Abstract

As great differences were observed in the amount of α-amylase in human saliva, there is a need to better understand the effect of this protein alone or in mixture with mucin on aroma compound partitioning. We report the respective role of mucin and α-amylase on the air/liquid partition coefficients of two series of 5 methyl-ketones and 5 ethyl-esters. We confirm that mucin affects the release of aroma compounds and, for the first time, we demonstrate the ability of α-amylase to decrease the release of aroma compounds. For both proteins, we report the involvement of hydrophobic effects. Interestingly, no cumulative effect was observed when both proteins were mixed together in solution. We hypothesize that protein–protein interactions occur between the two proteins and decrease the total number of available binding sites for aroma compounds. The effect of human saliva is also investigated and compared to that of artificial salivas. In the presence of human saliva the release of ketones is lower than in water and slightly higher than in the presence of artificial saliva composed of α-amylase and/or mucin. Esters are more affected by the presence of human saliva than ketones. This observation is due to the presence of an esterase activity in saliva, which activity increases with the hydrophobicity of esters. The difference observed in aroma release between artificial and human salivas could be explained by the presence of other salivary proteins in human saliva.

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