Importance Of Hydrophobicity In Functionality Of Food Proteins

Functional properties of food proteins have been defined as those characteristics, other than nutritional ones, that affect their utilization. This includes a diverse range of functionality, such as solubility, viscosity, water- and fat-binding properties, emulsification, foaming, film formation, gellability or coagulability, elasticity, and flavor. Functionality depends on the interaction of the protein molecules with other components in the food system, including water; macromolecules such as other proteins, complex carbohydrates, and lipids; and small molecules such as salts, simple sugars, and flavor compounds. These interactions may take place in the bulk phase, or at a surface or interface. The interplay of electrostatic, hydrophobic, and steric parameters, important in predicting biological activity of molecules (2), also holds true for the elucidation of the relationship between structure and functionality of food proteins (17,62). Computer-assisted studies for quantitative analysis of the structure—activity relationship (QSAR) of small molecules are widely applied (63), but progress in QSAR for functionality of food protein analyses has been much slower (62). Although the quali-

Table 2. Relative Hydrophobicity Values of Some Proteins Measured by Different Methods

Fluorescence probes DpH probe Chromatography _Binding_ Partition

Table 2. Relative Hydrophobicity Values of Some Proteins Measured by Different Methods

Fluorescence probes DpH probe Chromatography _Binding_ Partition

Proteins

H0 °

,S0ANS

S0CPA

S,,CPA

TG binding

Rpc

Hie

Heptane

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