Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page v
... Formation.................................. 16 V. Configuration and Conformation of Proteins at Interfaces..... 55 VI. Protein-Stabilized Foams...................................................................... 60 VII. Summary.........
... Formation.................................. 16 V. Configuration and Conformation of Proteins at Interfaces..... 55 VI. Protein-Stabilized Foams...................................................................... 60 VII. Summary.........
Page 1
... Conformation on Adsorption Electrostatic Effects Role of Water Structure Reversibility V. Configuration and Conformation of Proteins at Interfaces VI. Protein-Stabilized Foams A. Stability of Foams B. Methods for Measuring Foam ...
... Conformation on Adsorption Electrostatic Effects Role of Water Structure Reversibility V. Configuration and Conformation of Proteins at Interfaces VI. Protein-Stabilized Foams A. Stability of Foams B. Methods for Measuring Foam ...
Page 3
... conformational properties. These may include differences in amino acid sequence (which determines the secondary and tertiary structures), differences in the stability and/or flexibility of conformation to changes in the environment ...
... conformational properties. These may include differences in amino acid sequence (which determines the secondary and tertiary structures), differences in the stability and/or flexibility of conformation to changes in the environment ...
Page 12
... conformational state of the molecule. Once adsorbed, the subsequent behavior of the protein molecule in the adsorbed state depends on its conformational stability-flexibility under the prevailing thermodynamic conditions at the surface ...
... conformational state of the molecule. Once adsorbed, the subsequent behavior of the protein molecule in the adsorbed state depends on its conformational stability-flexibility under the prevailing thermodynamic conditions at the surface ...
Page 13
... conformational flexibility. If the free energy of activation of denaturation is greater than the excess free energy of the surface-interface, the rate of unfolding of the protein at the interface will be slow. On the other hand, if the ...
... conformational flexibility. If the free energy of activation of denaturation is greater than the excess free energy of the surface-interface, the rate of unfolding of the protein at the interface will be slow. On the other hand, if the ...
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