Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page 22
For the purpose of our discussion, we will consider only the adsorption
characteristics of 8-casein and lysozyme and relate these differences to
differences in their molecular characteristics. The time-dependent changes in the
surface pressure ...
For the purpose of our discussion, we will consider only the adsorption
characteristics of 8-casein and lysozyme and relate these differences to
differences in their molecular characteristics. The time-dependent changes in the
surface pressure ...
Page 23
Time-dependent changes in surface concentration (O) and surface pressure (O)
during the adsorption of (A) [3-casein and (B) lysozyme at the air-water interface.
The bulkphase protein concentrations were about 7.3 × 107* and 7.6 × 107% for
...
Time-dependent changes in surface concentration (O) and surface pressure (O)
during the adsorption of (A) [3-casein and (B) lysozyme at the air-water interface.
The bulkphase protein concentrations were about 7.3 × 107* and 7.6 × 107% for
...
Page 39
It was shown that the rate of adsorption of the positively charged lysozyme into
these monolayers decreased with time because of changes in the electrical
potential at the surface as a result of lysozyme adsorption. Comparison of the
initial ...
It was shown that the rate of adsorption of the positively charged lysozyme into
these monolayers decreased with time because of changes in the electrical
potential at the surface as a result of lysozyme adsorption. Comparison of the
initial ...
Page 58
fl-Casein Lysozyme 4 - - - # ----- 3% - - - - - FIG. 30. Schematic representation of
the configurations of 8-casein and lysozyme at the air-water interface at various
surface concentrations (T). 8-Casein: (1) T ~ 1 mg/m', (2) T = 1 mg/m', (3) T = Tot,
...
fl-Casein Lysozyme 4 - - - # ----- 3% - - - - - FIG. 30. Schematic representation of
the configurations of 8-casein and lysozyme at the air-water interface at various
surface concentrations (T). 8-Casein: (1) T ~ 1 mg/m', (2) T = 1 mg/m', (3) T = Tot,
...
Page 61
Rate of increase of foam volume of 3-casein (A), BSA (O), and lysozyme (D).
Protein concentration was 0.1% in 0.1 M NaCl. [From Graham and Phillips (1976)
. Reproduced with permission from Academic Press.] interface (Cumper, 1953;
Mita ...
Rate of increase of foam volume of 3-casein (A), BSA (O), and lysozyme (D).
Protein concentration was 0.1% in 0.1 M NaCl. [From Graham and Phillips (1976)
. Reproduced with permission from Academic Press.] interface (Cumper, 1953;
Mita ...
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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