Download Structure–Function Properties of Food Proteins by Lance G. Phillips PDF

By Lance G. Phillips

The practical homes of nutrition proteins have an effect on habit in nutrition platforms and impression the standard attributes, constitution, texture, mouth-feel, and style of the ultimate product. those attributes are accurately people with which meals engineers and technologists are involved whilst constructing new items. This leading edge booklet presents an outline of the actual homes of proteins and the way dynamic adjustments in conformation, structural adjustments, and protein-protein interactions are eager about the functionality of specific useful homes corresponding to gelation, emulsification, and foaming houses. versions used contain B-Lactoglobulin, soy, and meat proteins

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This requires energy, and is the basis of repulsive hydration forces (Parsegian, 1982; Saenger, 1987). Hydrating water also gives rise to hydrophobic interactions that stabilize the core of globular proteins. The hydrogen bonds between water and pro­ tein polar groups exert a stabilizing effect on protein structure provided the binding enthalpy is much greater than the free energy lost by the immobi­ lized solvent molecules (Janin, 1984; Schellman, 1987). 0 -1,207 -2,080 5130 -873 Abbreviations: PTI, pancreatic trypsin inhibitor; CPV, carp parvalbumin; RSA, ribonuclease A; LYZ, hen egg white lysozyme; MBN, sperm whale myoglobin; LZM, T 4 lysozyme; PAP; papain; CAB, carbonic anhydrase.

V. Protein-Water Interactions 35 about 5% more water than freeze-dried ß-lg (Bull and Breese, 1968; Fennema, 1977). However, surface area alone cannot provide an accurate description of protein hydration because denatured proteins have a greater surface area and generally tend to bind greater than 10% more water than native proteins. Serum albumin binds 33 and 46 g H 2 0 per gram protein in the native and denatured states, respectively. Thus, other features of protein structures are also responsible for water sorption and hydration properties, such as accessible surface polarity and hydrophobicity, as well as surface area and topography (Kinsella and Fox, 1986).

The magnitude of strength anions exert on the structure of water is apparently related to a progressive increase in the entropy with increasing ionic radius, suggesting that the entropy gain may arise primarily because large ions, with lower charge density on the surface, tend to break the hydrogen bonded framework of water (Table VI) (Hatefì and Hanstein, 1969; Damodaran and Kinsella, 1982). The data on proton NMR shifts and water self diffusion are also in agreement with this interpretation. Thus, both the increased shielding of water protons and the increased mobility of water molecules imply breaking of water structure (Hatefì and Hanstein, 1969).

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