By Lance G. Phillips
The practical houses of meals proteins impact habit in meals platforms and impact the standard attributes, constitution, texture, mouth-feel, and taste of the ultimate product. those attributes are accurately people with which nutrition engineers and technologists are involved whilst constructing new items. This leading edge booklet offers an summary of the actual homes of proteins and the way dynamic alterations in conformation, structural alterations, and protein-protein interactions are eager about the functionality of specific useful houses reminiscent of gelation, emulsification, and foaming homes. versions used comprise B-Lactoglobulin, soy, and meat proteins
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Extra info for Structure–Function Properties of Food Proteins
An ordered formation of hydration water molecules surrounding the methyl group of Ala 92 in human lysozyme has been observed (Blake et al, 1983). Four water molecules are in hydrogen-bonding contact and form a cyclic structure with the methyl group at the center. Structured water mole cules may be preferred around hydrophobic core residues; however, such assemblies are rarely seen in X-ray electron density maps because they are only visible with certain configurations of functional groups and at high reso lution (Saenger, 1987).
28 2. Protein Stability the thermodynamic properties of liquid hydrocarbons in water (Table II) (Privalov, 1979; Baldwin, 1986; Kauzmann, 1987). The difference in heat capacities has also been attributed to the "iceberg" model of water structure surrounding folded and unfolded protein molecules, that is, when nonpolar molecules are transferred into water, they induce in the layer of water mole cules immediately surrounding them hydrogen-bonded, ordered "cage-like" structures (decrease in entropy): as the temperature is raised, this "iceberg" gradually melts, thus accounting for the large contribution to the specific heat capacity of the protein molecule (Dill, 1985).
15 M) cause an increase in the amount of water bound to proteins. At higher concentrations of monovalent ions (2 M), protein hydration decreases because at this con centration ions compete with protein groups for water binding sites, sup press the electrical double layer surrounding the protein, and probably alter protein conformation (Kuntz and Kauzmann, 1974; Damodaran and Kinsella, 1982). However, the magnitude of the effects of salts vary with the cation and anion species involved and is related to the size of their respective hydrated radii; smaller hydrated radii have a greater charge density and hence produce a greater dehydration of the protein, which is generally in the order: Li+ >Na+ >K+ >Cs+ >Ca2+.
Structure–Function Properties of Food Proteins by Lance G. Phillips