Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
From inside the book
Results 6-10 of 91
Page 9
... interaction. While the first two interactions facilitate positive adsorption of the solute, the third factor would tend to promote negative adsorption at the interface. If the net free energy change (AG) of these three factors is ...
... interaction. While the first two interactions facilitate positive adsorption of the solute, the third factor would tend to promote negative adsorption at the interface. If the net free energy change (AG) of these three factors is ...
Page 13
... interactions emanating from various groups within the protein molecule and the interactions of the constituent amino acid residues with the surrounding solvent medium. The various noncovalent interactions which contribute positively to ...
... interactions emanating from various groups within the protein molecule and the interactions of the constituent amino acid residues with the surrounding solvent medium. The various noncovalent interactions which contribute positively to ...
Page 14
from hydrogen bonding, electrostatic, hydrophobic, and van der Waals dispersion interactions, respectively. The ... interaction that greatly restricts the flexibility and promotes stability of globular proteins is the disulfide bond ...
from hydrogen bonding, electrostatic, hydrophobic, and van der Waals dispersion interactions, respectively. The ... interaction that greatly restricts the flexibility and promotes stability of globular proteins is the disulfide bond ...
Page 15
... interactions. According to Bigelow (1967), proteins with lower average hydrophobicity and higher charge frequency ... interaction with the surrounding solvent are more important for its solubility characteristics than the global average ...
... interactions. According to Bigelow (1967), proteins with lower average hydrophobicity and higher charge frequency ... interaction with the surrounding solvent are more important for its solubility characteristics than the global average ...
Page 25
... interactions at the interface to form a continuous cohesive film. However, although the comparative studies on three different proteins, viz, 3-casein, bovine serum albumin, and lysozyme, did show that the conformation of proteins ...
... interactions at the interface to form a continuous cohesive film. However, although the comparative studies on three different proteins, viz, 3-casein, bovine serum albumin, and lysozyme, did show that the conformation of proteins ...
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