Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page 22
... effect of spread protein monolayers on the surface tension of water (for reviews, see James and Augenstein, 1966; Miller and Bach, 1973; MacRitchie, 1978). Since such studies do not represent the dynamic process of transport and ...
... effect of spread protein monolayers on the surface tension of water (for reviews, see James and Augenstein, 1966; Miller and Bach, 1973; MacRitchie, 1978). Since such studies do not represent the dynamic process of transport and ...
Page 43
... effect of ionic strength on the rate and extent of adsorption of the native and 99% succinylated 8-lactoglobulin as ... effects. To elucidate further the role of electrostatic interactions on the adsorption properties of succinylated 8 ...
... effect of ionic strength on the rate and extent of adsorption of the native and 99% succinylated 8-lactoglobulin as ... effects. To elucidate further the role of electrostatic interactions on the adsorption properties of succinylated 8 ...
Page 44
... Effect of ionic strength on the rate of change of surface pressure of native (3- lactoglobulin. 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 ...
... Effect of ionic strength on the rate of change of surface pressure of native (3- lactoglobulin. 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 ...
Page 46
... effect. It seems that, in order to overcome the unfavorable electrostatic barrier for adsorption, the protein might require a greater number of hydrophobic residues/segments to anchor itself at the interface. For example, assuming that ...
... effect. It seems that, in order to overcome the unfavorable electrostatic barrier for adsorption, the protein might require a greater number of hydrophobic residues/segments to anchor itself at the interface. For example, assuming that ...
Page 47
... effect. The origin of this effect is the thermodynamically unfavorable ordering of water molecules around the nonpolar portion of the solute, which decreases their entropy (Tanford, 1973). In other words, it can be surmised that the ...
... effect. The origin of this effect is the thermodynamically unfavorable ordering of water molecules around the nonpolar portion of the solute, which decreases their entropy (Tanford, 1973). In other words, it can be surmised that the ...
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