Future Trends

Long-term, systematic research is required to establish quantitative, empirical rules to understand the role of hydrophobicity in functionality of food protein systems. This basic research is required to explain at the molecular basis, various well-known but not clearly understood phenomena such as the thermostability of egg white foams, elasticity of egg white gels, coagulation of casein to form cheese, binding and texture formation of muscle proteins, elasticity and extensibility of wheat gluten dough, and so on.

Although only one of the physicochemical parameters involved in elucidation of structure-function relationships, hydrophobic interactions often play a key role. Improvement of functionality including whipping and emulsifying properties by modifying the hydrophobic-hydrophilic balance of proteins is exemplified in the preparation of pro-teinaceous surfactants with different HLB values by attachment of hydrophobic amino acid alkyl esters to various food proteins (78). Development of novel functionality such as antifreeze or cryoprotectant properties has also been described using this approach (78). Another rapidly developing area is the enhancement of hydrophobic nature of enzymes through attachment of amphiphilic groups such as poly(ethylene glycol), coupled with selection of organic solvent media to alter the hydrophobic environment. This area has interesting applications such as the possible resolution of alcohols and acids by lipase-catalyzed esterifi-cation, protease-catalyzed synthesis of proteins, and lipase-catalyzed interesterification of fats and oils (79). The potential of "ultrahydrophobic sequences" and betasheet structures of corn, wheat, and other proteins in film-forming preparations and adhesives (80) may be of value in the development of edible films. The growing market for reduced- and low-fat foods, which often have high protein content, suggests that more research should be undertaken to study the role of hydrophobic interactions in the binding and release of flavor compounds by food proteins.

Site-specific modifications of proteins can now be realized through molecular biology and genetic engineering techniques. By establishing the relationship between food protein structure and function, systematic and predictable enzyme and protein engineering for tailoring of specific biological and functional properties should become a reality.

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The Mediterranean Diet Meltdown

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