Modeling Bovine Serum Albumin Binding of Flavor Compounds (Alcohols, Aldehydes, Esters, and Ketones) as a Function of Molecular Properties
2008
Interactions between bovine serum albumin (BSA) and 4 classes of flavor compounds (alcohols, esters, aldehydes, and ketones) in aqueous solution were investigated using solid phase microextraction (SPME) of sample headspace and gas chromatography. Alcohols did not bind significantly to BSA. The binding of fixed amounts of individual flavor compounds with each functional group to increasing amounts of BSA was modeled as a function of several descriptors using partial least squares regression (PLSR). Ester binding was modeled as a function of the number of carbon atoms in a molecule and its boiling point (R²= 0.954). Aldehyde binding was modeled as a function of the number of hydrogen atoms and boiling point (R²= 0.922). Ketone binding was modeled as a function of the numbers of carbon atoms, length of the longer hydrocarbon chain, and degree of branching (R²= 0.961).
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