Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page 25
... concentration. [From Graham and Phillips (1979a). Reproduced with permission ... protein at the interface; the second kinetic phase, which evidently occurs ... protein adsorption. However, the relative magnitude of ki and k2 within a ...
... concentration. [From Graham and Phillips (1979a). Reproduced with permission ... protein at the interface; the second kinetic phase, which evidently occurs ... protein adsorption. However, the relative magnitude of ki and k2 within a ...
Page 38
... concentration (mg/mo. FIG. 13. Surface pressure versus surface concentration relationship of spread monolayers of ... protein concentration the diffusion step was rapid, below this concentration the rate of diffusion decreased ...
... concentration (mg/mo. FIG. 13. Surface pressure versus surface concentration relationship of spread monolayers of ... protein concentration the diffusion step was rapid, below this concentration the rate of diffusion decreased ...
Page 41
... concentration(malno acetyl, and succinyl B-casein in order to elucidate the influence of protein charge on the surface pressure isotherm. The net numbers of negative charges of 8-casein, acetyl 3-casein, and succinyl 8-casein were ...
... concentration(malno acetyl, and succinyl B-casein in order to elucidate the influence of protein charge on the surface pressure isotherm. The net numbers of negative charges of 8-casein, acetyl 3-casein, and succinyl 8-casein were ...
Page 42
... protein concentration was 2 x 107%. O, Native; e, 29% succinylated; [], 50% succinylated; E, 69% succinylated; A, 99% succinylated B-lactoglobulin. isoelectric pH of the protein. This has been attributed to decreased electrostatic ...
... protein concentration was 2 x 107%. O, Native; e, 29% succinylated; [], 50% succinylated; E, 69% succinylated; A, 99% succinylated B-lactoglobulin. isoelectric pH of the protein. This has been attributed to decreased electrostatic ...
Page 44
... 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 I O l 2 3 4 6 Time (h) FIG. 19. Effect of ionic strength on the rate of change of ...
... 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 I O l 2 3 4 6 Time (h) FIG. 19. Effect of ionic strength on the rate of change of ...
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