Conclusion

Various processing and environmental factors influence the functional properties of proteins; however, despite advances in molecular biology and analytical techniques the molecular basis for induced functional changes still remains ill defined. The reader is referred to articles by Jimenez-Flores and Bleck (112) and Yada et al. (113) for references regarding to recent advances in food biotechnology and analytical techniques, respectively. Although great gains have been made in the understanding of protein structure and its stabilization and, therefore, functionality, a need still exists to better define and characterize the denaturation of (specific) proteins if we are to control this phenomenon and take advantage of the technological attributes that proteins have to offer. Methodology by which to recognize denaturation when it occurs must be standardized. That food by its very nature is a multicomponent system in which a myriad of interactions can/have occurred makes this a foreboding task. Yet, in order to meet this mandate, the use of multicomponent or actual food systems is required. It must be stressed that although every protein has a unique structure and, therefore, unique conformational potential, the behavior of a protein in a given system is governed by thermodynamic and kinetic constraints.

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