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By Nicholas Parris, Akio Kato, Lawrence K. Creamer, John Pearce
content material: Structure-property relationships in meals / Vladimir Tolstoguzov --
Macromolecular interactions of foodstuff proteins studied through Raman spectroscopy : interactions of [beta]-lactoglobulin, [alpha]-lactalbumin, and lysozyme in resolution, gels, and precipitates / Eunice C.Y. Li-Chan --
components deciding on the nature of biopolymer-biopolymer interactions in multicomponent aqueous options modeling nutrients structures / M.G. Semenova --
Use of nonlinear regression for reading [beta]-lactoglobulin denaturation kinetics in skim milk / D.J. Oldfield, Harjinder Singh, M.W. Taylor, and K.N. Pearce --
Particle sizes of casein submicelles and purified [kappa]-casein : comparisons of dynamic gentle scattering and electron microscopy with predictive 3-dimensional molecular versions / H.M. Farrell, Jr., P.H. Cooke, G. King, P.D. Hoagland, M.L. Groves, T.F. Kumosinski, and B. Chu --
results of divalent cations, phytic acid, and phenolic compounds at the gelation of ovalbumin and canola proteins / Susan D. Arntfield --
The position of [alpha]-lactalbumin in heat-induced gelation of whey proteins / N. Matsudomi and T. Oshita --
Laser-light-scattering homes of heat-induced ovalbumin gels / Yoshinori Mine --
Aggregation and gelation of bovine [beta]-lactoglobulin, [alpha]-lactalbumin, and serum albumin / Jacquiline Gezimati, Harjinder Singh, and Lawrence ok. Creamer --
Gelation houses of myosin : position of subfragments and actin / S.F. Wang, A.B. Smyth, and D.M. Smith --
results of macromolecular interactions at the permeability of composite fit for human consumption movies / Tara Habig McHugh --
motion pictures from pectin, chitosan, and starch / P.D. Hoagland --
Lipid-protein interplay at an emulsified oil floor : protein buildings and their roles in lipid binding / M. Shimizu and M. Saito --
features of the goods of restricted proteolysis of [beta]-lactoglobulin / Harold E. Swaisgood, Xiaolin L. Huang, and George L. Catignani --
results of excessive strain on protein-polysaccharide interactions / V.B. Galazka and D.A. Ledward --
Biopolymer interactions in emulsion platforms : impacts on creaming, flocculation, and rheology / Eric Dickinson --
Phosphorylation of proteins and their useful and structural homes / Fakhrieh Vojdani and John R. Whitaker --
development of useful houses of nutrition proteins through conjugation of glucose-6-phosphate / Takayoshi Aoki --
Novel sensible houses of glycosylated lysozymes built through chemical and genetic ameliorations / Akio Kato, S. Nakamura, H. Takasaki, and S. Maki --
Crystallization and X-ray research of ordinary and transformed recombinant soybean proglycinins : third-dimensional constitution of standard proglyeinin at 6 Å solution / S. Utsumi, A.B. Gidamis, Y. Takenaka, N. Maruyama, M. Adachi, and B. Mikami --
a few features of a microbial protein cross-linking enzyme : transglutaminase / Katsuya Seguro, Noriki Nio, and Masao Motoki --
impression of the bovine [beta]-lactoglobulin phenotype at the homes of [beta]-lactoglobulin, milk composition, and dairy items / Jeremy P. Hill, Mike J. Boland, Lawrence okay. Creamer, Skelte G. Anema, Don E. Otter, Geoff R. Paterson, Ruth Lowe, Rose L. movement, and Wayne C. Thresher.
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Extra info for Macromolecular Interactions in Food Technology
Sample text
Table IX. 56 Caseinate 4 4 Interactions between different biopolymers becomes more favorable in the presence of the sucrose. Presumably, because of both the decrease of the excluded volume effect as a result of the Caseinate molecular weight reducing and rise of the Caseinate hydrophobicity. This change of character of the interactions between proteins under the influence of sucrose leads to the increase of the concentration of the protein's miscibility, especially under low concentration of the Caseinate molecule in the solution ( See Figure 4).
Macromolecules. 1992, 25, 1493 - 1502. 15. ; Lindman, B. Advancea in Colloid and Interface Science. 1992, 41, 149- 178. ; ACS Symposium Series; American Chemical Society: Washington, DC, 1996. Chapter 4 Use of Nonlinear Regression for Analyzing β-Lactoglobulin Denaturation Kinetics in Skim Milk 1 1 1 2 D. Oldfield ,Harjinder Singh , M. Taylor ,and K. N. ch004 1 Department of Food Technology, Massey University, Palmerston North, New Zealand New Zealand Dairy Research Institute, Private Bag 11029, Palmerston North, New Zealand 2 Five different methods were used to calculate the kinetic parameters for the denaturation ofβ-lactoglobulin(genetic variant A).
Ch003 a 3 A 2 = N 10' [2k(R 23 A 2 3 + R)l 3 + 4n/3(R + R ) ], 2 2 (7) 3 where N is Avogadro's number; R is rod cylindrical radius an hemispherical ends of radius R ; 1 is half-length of the rod cylinder; R3 is equivalent hard sphere radius. It should be pointed out that an equivalent hard sphere corresponds to the space occupied in aqueous medium by one biopolymer which is absolutely not accessible for other biopolymers (10). For the calculation of the radius of the equivalent hard sphere in some cases it is necessary to use a penetration parameter which is specific for different conformations of macromolecules.