Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page 38
... ionic strength (Tornberg, 1978a). In contrast, whey proteins diffused faster but spread slower in 0.2 M NaCl than in water. In the case of the caseinate the diffusion-limited absorption was shown to be concentration dependent. While ...
... ionic strength (Tornberg, 1978a). In contrast, whey proteins diffused faster but spread slower in 0.2 M NaCl than in water. In the case of the caseinate the diffusion-limited absorption was shown to be concentration dependent. While ...
Page 41
... pressure versus surface concentration relationship of native (O) and 69% succinylated (A) [3-lactoglobulin. FIG. 20. Relationship between steady-state surface pressure and ionic strength: INTERFACES, PROTEIN FILMS, AND FOAMS 41.
... pressure versus surface concentration relationship of native (O) and 69% succinylated (A) [3-lactoglobulin. FIG. 20. Relationship between steady-state surface pressure and ionic strength: INTERFACES, PROTEIN FILMS, AND FOAMS 41.
Page 43
... ionic strength of the medium. In the case of native 3-lactoglobulin, the major increase in the rate and steady-state surface pressure values occurred up to 0.2 ionic strength; increase of ionic strength from 0.2 to 0.4 caused only ...
... ionic strength of the medium. In the case of native 3-lactoglobulin, the major increase in the rate and steady-state surface pressure values occurred up to 0.2 ionic strength; increase of ionic strength from 0.2 to 0.4 caused only ...
Page 44
... ionic strength on the rate of change of surface pressure of native (3- lactoglobulin. Protein concentration was 2 × 10^*%. Ionic strength: O, 0.038; II, 0.05; A, (). : @, 0.2: [], (). 4. g 20|- z 5 © 5 o go * c. 10}- Q o s s go i | # l ...
... ionic strength on the rate of change of surface pressure of native (3- lactoglobulin. Protein concentration was 2 × 10^*%. Ionic strength: O, 0.038; II, 0.05; A, (). : @, 0.2: [], (). 4. g 20|- z 5 © 5 o go * c. 10}- Q o s s go i | # l ...
Page 45
... Ionic strength nonlinear for all the 3-lactoglobulin derivatives (Fig. 21). However, as in the case of BSA intermediates (Fig. 11), the curves in Fig. 21 exhibit distinct breaking points, indicating that two molecular processes, namely ...
... Ionic strength nonlinear for all the 3-lactoglobulin derivatives (Fig. 21). However, as in the case of BSA intermediates (Fig. 11), the curves in Fig. 21 exhibit distinct breaking points, indicating that two molecular processes, namely ...
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