Food flavor is one of the decisive factors for consumers to purchase and receive food. Flavor depends on the concentration of various volatile components in the headspace, the threshold, etc., and the temperature, the vapor pressure of volatile components, and other food components. Interaction related. At present, the study of flavor mainly focuses on the formation mechanism of flavor components, and there are few reports on the relationship between the release and perception of flavor components and the determination of their content by protein assays.

Amino acid is an important component of protein. The diversity of its side chain structure makes the protein and volatile flavor components have a variety of forces, most of which are reversible binding, including ionic bonds, hydrogen bonds, and hydrophobic interactions; The covalent bond functions as an irreversible bond, which mainly includes the amino groups of the aldehyde and lysine residue side chains, amines and carboxyl groups, and the binding of sulfur-containing compounds to proteins. Therefore, the measured value of the protein analyzer has a certain relationship with the above factors and the number of amino groups.

The binding mechanism of protein and volatile flavor components has yet to be further studied by the protein analyzer, especially the conformational changes of the protein at the site of action and before and after the action. At present, β-lactoglobulin as a research model has not yet been elucidated. Many researchers used Fourier transform infrared spectroscopy, nuclear magnetic resonance, equilibrium dialysis and other analytical methods to study the β-lactoglobulin flavor binding sites, confirming that the β-lactoglobulin flavor binding sites are mostly distributed in hydrophobic regions of proteins. And there are multiple different binding sites as well as weaker secondary binding sites.

The content determination by the protein analyzer is related to the above types of action and the composition and properties of the proteins and volatile components. There is no uniform binding mechanism, and most of them are characterized by the reversible effects of hydrophobicity, which is also the special folding and protein of the polypeptide chain. The structure tends to be stable. The use of reversible binding can reduce the flavor loss during the processing and re-release the flavor components when consumed, and the reversible combination is important for removing odors in the food.

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