Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page 3
... changes in the environment, symmetric or asymmetric distribution of polar and nonpolar batches on the surface of the molecule, and molecular size and shape. All of these molecular properties will collectively influence the film-forming ...
... changes in the environment, symmetric or asymmetric distribution of polar and nonpolar batches on the surface of the molecule, and molecular size and shape. All of these molecular properties will collectively influence the film-forming ...
Page 9
... change caused by the hydrophobic group. If the free energy change for the water-hydrophilic group interaction is more negative than the positive free energy change for the water-hydrocarbon chain interaction, then the solute molecule ...
... change caused by the hydrophobic group. If the free energy change for the water-hydrophilic group interaction is more negative than the positive free energy change for the water-hydrocarbon chain interaction, then the solute molecule ...
Page 10
... change for transfer of a methylene group from an organic phase into the aqueous phase, which is about 3.57 kJ/mol (Tanford, 1973; McAuliffe, 1966; Smith and ... changes within water. The higher the chain length. 10 SRINIVASAN DAMODARAN.
... change for transfer of a methylene group from an organic phase into the aqueous phase, which is about 3.57 kJ/mol (Tanford, 1973; McAuliffe, 1966; Smith and ... changes within water. The higher the chain length. 10 SRINIVASAN DAMODARAN.
Page 11
the entropy changes within water. The higher the chain length (or the surface area) of the hydrophobic solute, the greater would be the entropy change and the free energy of adsorption. The fact that the free energy of adsorption of ...
the entropy changes within water. The higher the chain length (or the surface area) of the hydrophobic solute, the greater would be the entropy change and the free energy of adsorption. The fact that the free energy of adsorption of ...
Page 13
... TAS-ons (10) where AGh, AGele, AGho, and AG, aware the free energy changes emanating from hydrogen bonding, electrostatic, hydrophobic, and van der Waals dispersion INTERFACES, PROTEIN FILMS, AND FOAMS 13 III. Protein Structure.
... TAS-ons (10) where AGh, AGele, AGho, and AG, aware the free energy changes emanating from hydrogen bonding, electrostatic, hydrophobic, and van der Waals dispersion INTERFACES, PROTEIN FILMS, AND FOAMS 13 III. Protein Structure.
Contents
81 | |
Chapter 3 The Gelation of Proteins | 203 |
A Molecular Basis for Modeling Biomacromolecular Processes | 299 |
Chapter 5 Meat Mutagens | 387 |
Index | 451 |
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8-lactoglobulin acid phosphatase adsorbed adsorption aggregation Agric air-water interface amino acid analysis aqueous beef behavior binding bovine bovine serum albumin calcium casein cell walls changes Chattoraj cheese coalescence Colloid Colloid Interface Sci conformation constant creaming cross-links decrease denaturation droplets effect elasticity electrostatic emulsifying emulsifying properties emulsion stability emulsions enzyme equation film flocculation foam food emulsions Food Sci formed free energy functional properties gelatin gelatin gels gelation globulin Graham and Phillips heat-induced heating Hermansson increase interactions interfacial tension ionic strength k-casein kinetics Kinsella liquid lysozyme MacRitchie meat microemulsion modulus molecular molecule monolayers mutagen formation mutagenic mutagenic activity myosin NaCl nonlinear regression oil/water interface ovalbumin phase polymer protein concentration protein gels residues rheological salt serum albumin solubility solution solvent soy protein structure studies succinylated surface pressure surfactants Table temperature thermodynamic tion values viscosity whey protein