Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page vi
... .............................................. 30| !!!. Casein Colloidai Stability Profiles............................................................ 325 IV. Gel Strength of Whey Protein Isolate...........................
... .............................................. 30| !!!. Casein Colloidai Stability Profiles............................................................ 325 IV. Gel Strength of Whey Protein Isolate...........................
Page 14
... casein, and 17 out of 199 residues in a-casein are proline residues (Swaisgood, 1982). The uniform distribution of these residues in the primary structure prevents formation of ordered structures in these proteins. Many physicochemical ...
... casein, and 17 out of 199 residues in a-casein are proline residues (Swaisgood, 1982). The uniform distribution of these residues in the primary structure prevents formation of ordered structures in these proteins. Many physicochemical ...
Page 19
... casein (D) and k-casein (O) to the air-water interface. Bulk-phase protein concentrations were 107% and 1.5 × 107% for acetyl-3-casein and kcasein, respectively. [From Benjamins et al. (1975). Reproduced with permission from the ...
... casein (D) and k-casein (O) to the air-water interface. Bulk-phase protein concentrations were 107% and 1.5 × 107% for acetyl-3-casein and kcasein, respectively. [From Benjamins et al. (1975). Reproduced with permission from the ...
Page 20
... Casein 1.0 x 107* 3.30 0.7b Stirred k-Casein 1.5 × 10^* 1,50 1.0% Stirred Ovalbumin 1.0 x 10-4 0.5° 0.7d Unstirred Lysozyme 1.0 × 10−" 0.2% 1.04 Unstirred " From Benjamins et al. (1975). " From Smith (1968). ' From DeFeijter and ...
... Casein 1.0 x 107* 3.30 0.7b Stirred k-Casein 1.5 × 10^* 1,50 1.0% Stirred Ovalbumin 1.0 x 10-4 0.5° 0.7d Unstirred Lysozyme 1.0 × 10−" 0.2% 1.04 Unstirred " From Benjamins et al. (1975). " From Smith (1968). ' From DeFeijter and ...
Page 22
... casein and 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 ...
... casein and 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 ...
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