Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page 19
... lysozyme, in which the experiments were done without stirring, the diffusion coefficients obtained from adsorption experiments were significantly lower than the literature values, and certainly beyond the experimental error of the ...
... lysozyme, in which the experiments were done without stirring, the diffusion coefficients obtained from adsorption experiments were significantly lower than the literature values, and certainly beyond the experimental error of the ...
Page 20
... Lysozyme 1.0 × 10−" 0.2% 1.04 Unstirred " From Benjamins et al. (1975). " From Smith (1968). ' From DeFeijter and Benjamins (1987). * From Tanford (1961). B. ENERGY BARRIER THEORY In many adsorption studies on proteins, the rates of ...
... Lysozyme 1.0 × 10−" 0.2% 1.04 Unstirred " From Benjamins et al. (1975). " From Smith (1968). ' From DeFeijter and Benjamins (1987). * From Tanford (1961). B. ENERGY BARRIER THEORY In many adsorption studies on proteins, the rates of ...
Page 22
... lysozyme and relate these differences to differences in their molecular characteristics. The time-dependent changes in the surface pressure and surface concentration of dilute solutions of 3-casein and lysozyme are shown in Fig. 6 ...
... lysozyme and relate these differences to differences in their molecular characteristics. The time-dependent changes in the surface pressure and surface concentration of dilute solutions of 3-casein and lysozyme are shown in Fig. 6 ...
Page 23
... lysozyme at the air-water interface. The bulkphase protein concentrations were about 7.3 × 107* and 7.6 × 107% for 3-casein and lysozyme, respectively. [From Graham and Phillips (1979a). Reproduced with permission from Academic Press ...
... lysozyme at the air-water interface. The bulkphase protein concentrations were about 7.3 × 107* and 7.6 × 107% for 3-casein and lysozyme, respectively. [From Graham and Phillips (1979a). Reproduced with permission from Academic Press ...
Page 24
TABLE IV DIFFERENCES IN THE MOLECULAR PROPERTIES OF 3-CASEIN AND LYSOZYME Property £8-Casein Lysozyme Molecular weight 24,000 14,500 o-Helical structure (%) 10 46 B-Sheet structure (%) - 19 Tertiary structure Flexible, random Rigid ...
TABLE IV DIFFERENCES IN THE MOLECULAR PROPERTIES OF 3-CASEIN AND LYSOZYME Property £8-Casein Lysozyme Molecular weight 24,000 14,500 o-Helical structure (%) 10 46 B-Sheet structure (%) - 19 Tertiary structure Flexible, random Rigid ...
Contents
Physicochemical Role of Protein and Nonprotein Emulsifiers | 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