Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page vi
... .................................... 299 II. Protein Salt-Induced Solubility Profiles.................................................... 30| !!!. Casein Colloidai Stability Profiles...................................
... .................................... 299 II. Protein Salt-Induced Solubility Profiles.................................................... 30| !!!. Casein Colloidai Stability Profiles...................................
Page 47
... salts such as NaF and Na2S04 increase the structure of bulk water (kosmotropes) and salts such as NaC104 and NaSCN break the normal hydrogen-bonded structure of water (chaotropes) (Dandliker and de Saussure, 1971; von Hippel and ...
... salts such as NaF and Na2S04 increase the structure of bulk water (kosmotropes) and salts such as NaC104 and NaSCN break the normal hydrogen-bonded structure of water (chaotropes) (Dandliker and de Saussure, 1971; von Hippel and ...
Page 48
... salts can be employed to change the state of bulk water structure and study its effect on protein adsorption. However, one of the difficulties of this approach is that the addition of a chaotropic salt to a protein solution would not ...
... salts can be employed to change the state of bulk water structure and study its effect on protein adsorption. However, one of the difficulties of this approach is that the addition of a chaotropic salt to a protein solution would not ...
Page 49
... salt concentration resulted in increase of surface pressure (Fig. 26); however, the extent of increase of surface pressure with salt concentration was greater with NaCl than with NaSCN. Comparison of the data in Figs. 25 and 26 suggests ...
... salt concentration resulted in increase of surface pressure (Fig. 26); however, the extent of increase of surface pressure with salt concentration was greater with NaCl than with NaSCN. Comparison of the data in Figs. 25 and 26 suggests ...
Page 50
... Salt. FIG. 23. Rate of adsorption of 3-casein at the air-water interface in the presence of 1 M V. CONFIGURATION AND CONFORMATION OF PROTEINS AT INTERFACES FIG. 32. log Co FIG. 24. Adsorption isotherms of 8-casein in the presence of 1 M ...
... Salt. FIG. 23. Rate of adsorption of 3-casein at the air-water interface in the presence of 1 M V. CONFIGURATION AND CONFORMATION OF PROTEINS AT INTERFACES FIG. 32. log Co FIG. 24. Adsorption isotherms of 8-casein in the presence of 1 M ...
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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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