ABSTRACT
Hydrophobicity scales that have been published can be classified into two groups: those derived from solubility measurement and those calculated empirically from the molecular structure, especially X-ray patterns, based on the assumption that hydrophobic amino acid residues are buried in the interior of protein molecules. Hydrophobic probe methods may be the simplest type of method for measuring protein hydrophobicity. Among many hydrophobic probes which have been used so far, 1-anilinonaphthalene-8-sulfonate (ANS) is the most frequently used probe. Binding of sodium dodecylsulfate (SDS) with proteins is primarily hydrophobic in nature. The presence of groups that tend to withdraw electrons, e.g., carboxyl, azo and nitro groups and halides, usually quenches fluorescence. It is, however, unlikely that very useful quantitative information will be obtained on the overall protein hydrophobicity by using this method. Hydrocarbon binding capacity is rather difficult to relate to similar phenomena in food systems, except for flavor study, e.g., adsorption of aroma compounds with food macro-molecules.
