Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page 12
... temperature), the molecule would adsorb to the surface-interface. The number of segments that are involved in the attachment of the protein to the surface and the free energy of adsorption of the segments depend on the various molecular ...
... temperature), the molecule would adsorb to the surface-interface. The number of segments that are involved in the attachment of the protein to the surface and the free energy of adsorption of the segments depend on the various molecular ...
Page 14
... temperature and AScout is the conformational entropy, is the unfavorable (meaning positive) free energy change resulting from the loss of conformational entropy of the polypeptide. The net thermodynamic stability of the native structure ...
... temperature and AScout is the conformational entropy, is the unfavorable (meaning positive) free energy change resulting from the loss of conformational entropy of the polypeptide. The net thermodynamic stability of the native structure ...
Page 21
... temperature. For an irreversible adsorption process the second term of equation can be omitted. Replacement of activity with concentration gives dT/dt = k1Co exp(-tt AA/kT) (17) Comparison of Eqs. (14) and (17) indicates that Eq. (17) ...
... temperature. For an irreversible adsorption process the second term of equation can be omitted. Replacement of activity with concentration gives dT/dt = k1Co exp(-tt AA/kT) (17) Comparison of Eqs. (14) and (17) indicates that Eq. (17) ...
Page 24
... temperature (°C) Isoelectric pH 4.6 ~ 1 1.0 flexible and random-coil nature, upon adsorption at the air-water interface, 3-casein readily unfolds, reorients, spreads at the interface and occupies a greater area per molecule at the ...
... temperature (°C) Isoelectric pH 4.6 ~ 1 1.0 flexible and random-coil nature, upon adsorption at the air-water interface, 3-casein readily unfolds, reorients, spreads at the interface and occupies a greater area per molecule at the ...
Page 56
... temperature, and 6 is the degree of surface coverage which is equal to ao/a, where a is the observed area per statistical unit (which is given by 1/Tn where T is the surface concentration of the protein and n is the number of amino acid ...
... temperature, and 6 is the degree of surface coverage which is equal to ao/a, where a is the observed area per statistical unit (which is given by 1/Tn where T is the surface concentration of the protein and n is the number of amino acid ...
Contents
81 | |
Chapter 3 The Gelation of Proteins | 203 |
A Molecular Basis for Modeling Biomacromolecular Processes | 299 |
Chapter 5 Meat Mutagens | 387 |
Index | 451 |
Common terms and phrases
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