Advances in Food and Nutrition Research, Volume 34Advances in Food and Nutrition Research |
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Page 18
... bovine serum albumin as 6.0 x 10−" cm3/sec, MacRitchie and Alexander (1963a) calculated the time taken to reach various surface pressures at a given bulk protein concentration and compared the predicted values with the actual ...
... bovine serum albumin as 6.0 x 10−" cm3/sec, MacRitchie and Alexander (1963a) calculated the time taken to reach various surface pressures at a given bulk protein concentration and compared the predicted values with the actual ...
Page 22
... bovine serum albumin, and 3-casein, at the air-waterinterface by monitoring the rate of change of surface concentration and surface pressure simultaneously. For the purpose of our discussion, we will consider only the adsorption ...
... bovine serum albumin, and 3-casein, at the air-waterinterface by monitoring the rate of change of surface concentration and surface pressure simultaneously. For the purpose of our discussion, we will consider only the adsorption ...
Page 25
... bovine serum albumin at the air-water interface also followed similar biphasic first-order kinetics (Song and Damodaran, 1987), indicating that the biphasic behavior is a general rule rather than an exception for globular protein ...
... bovine serum albumin at the air-water interface also followed similar biphasic first-order kinetics (Song and Damodaran, 1987), indicating that the biphasic behavior is a general rule rather than an exception for globular protein ...
Page 26
... bovine serum albumin and seven intermediates at the air-water interface. The substrate was 20 mM sodium phosphate buffer, pH 7.0. The bulk concentrations of various intermediates were O, intermediate 1, 0.308 × 10^*%; A, intermediate 2 ...
... bovine serum albumin and seven intermediates at the air-water interface. The substrate was 20 mM sodium phosphate buffer, pH 7.0. The bulk concentrations of various intermediates were O, intermediate 1, 0.308 × 10^*%; A, intermediate 2 ...
Page 27
TABLE V CONFORMATIONAL PROPERTIES OF BOVINE SERUM ALBUMIN INTERMEDIATES" [6]+, [6]221 recovery Number of Intermediate (deg cm dimol ')” (%) S–S bonds l –7,963 36.0 0 2 – 10,496 49.5 6.5 3 –6,100 28.7 8.5 4 – 15,300 72. I 12.7 5 — 19,160 ...
TABLE V CONFORMATIONAL PROPERTIES OF BOVINE SERUM ALBUMIN INTERMEDIATES" [6]+, [6]221 recovery Number of Intermediate (deg cm dimol ')” (%) S–S bonds l –7,963 36.0 0 2 – 10,496 49.5 6.5 3 –6,100 28.7 8.5 4 – 15,300 72. I 12.7 5 — 19,160 ...
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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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