Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
From inside the book
Page 19
... ovalbumin and 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 ...
... ovalbumin and 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 ...
Page 20
... 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 Benjamins (1987). * From Tanford (1961). B. ENERGY BARRIER THEORY In many ...
... 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 Benjamins (1987). * From Tanford (1961). B. ENERGY BARRIER THEORY In many ...
Page 29
... ovalbumin (Mr = 45,000). Since the frictional coefficient is proportional to the cube root of molecular weight, on the basis of Eq. (22) one would expect the D, of lysozyme to be greater than that of ovalbumin. Assuming that the ...
... ovalbumin (Mr = 45,000). Since the frictional coefficient is proportional to the cube root of molecular weight, on the basis of Eq. (22) one would expect the D, of lysozyme to be greater than that of ovalbumin. Assuming that the ...
Page 60
... ovalbumin reacted with DTNB, indicating that a conformational change in the ovalbumin occurred during foaming. Although these reports tentatively confirm that adsorption of proteins at the air-water interface causes interfacial ...
... ovalbumin reacted with DTNB, indicating that a conformational change in the ovalbumin occurred during foaming. Although these reports tentatively confirm that adsorption of proteins at the air-water interface causes interfacial ...
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