Chemical and Instrumental Characterization of Protein–Flavor Interactions

Abstract

In all fields of science, the ability to advance understanding and knowledge is tied to the ability to measure outcomes. As early as 1920, it was observed that the composition of a food influences the sensory perception of aroma compounds added to it. However, it was not until the early 1960s that gas chromatographic instrumentation became available to measure how and what was responsible for influencing flavor perception as the food composition was altered. The early methods were fairly simple, depending on headspace analysis to gain an understanding. Headspace methodologies lacked sensitivity to work in the range of human perception on many aroma compounds, and thus, more sensitive methods were developed, such as equilibrium dialysis and headspace concentration techniques. The most recent developments in this area employ sophisticated mass spectrometry to measure how flavor compounds react with food proteins and where they react within the protein. This chapter tracks the development of methodology and learning focusing on both weak (ionic, hydrophilic, and hydrophobic) and strong (covalent) bonding of flavor compounds to various protein sources.