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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 nutrients proteins studied by means of Raman spectroscopy : interactions of [beta]-lactoglobulin, [alpha]-lactalbumin, and lysozyme in answer, gels, and precipitates / Eunice C.Y. Li-Chan --
components selecting the nature of biopolymer-biopolymer interactions in multicomponent aqueous ideas modeling nutrients structures / M.G. Semenova --
Use of nonlinear regression for interpreting [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 mild scattering and electron microscopy with predictive third-dimensional molecular types / 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 homes 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 --
movies 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 structures : 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 by means of conjugation of glucose-6-phosphate / Takayoshi Aoki --
Novel practical homes of glycosylated lysozymes built via chemical and genetic variations / Akio Kato, S. Nakamura, H. Takasaki, and S. Maki --
Crystallization and X-ray research of ordinary and converted recombinant soybean proglycinins : 3-dimensional constitution of standard proglyeinin at 6 Å answer / 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 --
influence of the bovine [beta]-lactoglobulin phenotype at the houses 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 resources for Macromolecular Interactions in Food Technology

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SPIE Fourier Transform Spectroscopy 1989, 1145, 415-417. ; Kinsella, J. E. J. Agric. Food Chem. 1993, 41, 1053-1057. ; Castberg, H. B. J. Food Sci.. 1986, 57, 87-90. ; Foegeding, E. A. J. Agric. Food Chem. 1993, 41, 341-346. ; Bonomi, F. J. Agric. Food Chem. 1992, 40, 1731-1736. Legowo, A. M . ; Hayakawa, S. Food Research International 1993, 26, 103-108. Donovan, J. ; Mapes, C. ; Davis, J. ; Garibaldi, J. A. J. Sci. Food Agric. 1975, 26, 73-83. ; Nakamura, R. Agric. Biol. Chem. 1986, 50, 2039-2046.

The role of the charge in the interaction of the biopolymers is most significant when such parameters of the system as pH and ionic strength are varied. ; Semenova, M . G . ; Tsapkina, E . N . Food Hydrocolloids, in press) provides example of the effects of varying pH on the interactions between two globular proteins in solution. Table VI shows that the decrease in the net negative charge on the proteins when the pH is lowered caused sharp weakening of the intensity of the interactions between both the same and different protein molecules.

In other words, assuming that under electroneutral conditions space occupied by a semi-rigid chain polymer to a large extent is accessible to the protein globules in contrast to the space occupied by flexible-chain biopolymer. In consequence of this a marked decrease in contribution of the excluded volume effect in interaction of the biopolymers was observed. Increase in the order of magnitude of A23 were observed for interactions of the flexible-chain biopolymer. Dextran, with biopolymers in globular, rigid rod and semi-rigid rod conformations.

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