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Structures coagulation

The development of polymer chemistry was particularly important in the last, XX centaury. New types of polymers, with different properties, were obtained. They found application as construction materials, foils, synthetic fibers, S5mthetic rubbers, adhesives, ion exchangers, products to change the soil structure, coagulating agents, in medicines, electric conductors and semiconductors, photoconductors, etc. The diversity and versatility of polymers, provided by the possible infinite modification of their molecular and macroscopic structure guarantees a further development and increase of applications of these materials. [Pg.253]

The function of emulsifier in the emulsion polymerization process may be summarized as follows [45] (1) the insolubilized part of the monomer is dispersed and stabilized within the water phase in the form of fine droplets, (2) a part of monomer is taken into the micel structure by solubilization, (3) the forming latex particles are protected from the coagulation by the adsorption of monomer onto the surface of the particles, (4) the emulsifier makes it easier the solubilize the oligomeric chains within the micelles, (5) the emulsifier catalyzes the initiation reaction, and (6) it may act as a transfer agent or retarder leading to chemical binding of emulsifier molecules to the polymer. [Pg.196]

Denaturation is accompanied by changes in both physical and biological properties. Solubility is drastically decreased, as occurs when egg white is cooked and the albumins unfold and coagulate. Most enzymes also lose all catalytic activity when denatured, since a precisely defined tertiary structure is required for their action. Although most denaturation is irreversible, some cases are known where spontaneous renaturation of an unfolded protein to its stable tertiary structure occurs. Renaturation is accompanied by a full recovery of biological activity. [Pg.1040]

Similarly to blood coagulation, reactions of fibrinolysis occur on the interface of fluid-and solid-phase structures, generally in transiently formed compartments. [Pg.505]

This paper presents the physical mechanism and the structure of a comprehensive dynamic Emulsion Polymerization Model (EPM). EPM combines the theory of coagulative nucleation of homogeneously nucleated precursors with detailed species material and energy balances to calculate the time evolution of the concentration, size, and colloidal characteristics of latex particles, the monomer conversions, the copolymer composition, and molecular weight in an emulsion system. The capabilities of EPM are demonstrated by comparisons of its predictions with experimental data from the literature covering styrene and styrene/methyl methacrylate polymerizations. EPM can successfully simulate continuous and batch reactors over a wide range of initiator and added surfactant concentrations. [Pg.360]

The starting time for rheological measurements correspond to t = 120 min. Indeed, the rheological parameters were only recorded during the rennet-induced coagulation phase to avoid structural modifications during the acidification phase which may consequently influence the gelation process. Elastic and viscous properties of reconstituted milks... [Pg.278]

The six major proteins of milk, asl-, o s2-, and /c-casein, jS-lactoglobulin, and a-lactalbumin, contain at least one tryptophan residue [57], the fluorescence of which allows the monitoring of the structural modifications of proteins and their physicochemical environment during the coagulation processes. Emission fluorescence spectra of the protein tryptophanyl residues were recorded for the milk coagulation kinetics induced by... [Pg.281]

Structural Evolution During the Three Different Coagulation Processes... [Pg.285]


See other pages where Structures coagulation is mentioned: [Pg.469]    [Pg.253]    [Pg.469]    [Pg.253]    [Pg.1061]    [Pg.1441]    [Pg.1681]    [Pg.36]    [Pg.111]    [Pg.361]    [Pg.77]    [Pg.502]    [Pg.156]    [Pg.586]    [Pg.407]    [Pg.227]    [Pg.945]    [Pg.1030]    [Pg.51]    [Pg.152]    [Pg.2]    [Pg.34]    [Pg.441]    [Pg.121]    [Pg.656]    [Pg.420]    [Pg.135]    [Pg.476]    [Pg.42]    [Pg.42]    [Pg.52]    [Pg.37]    [Pg.272]    [Pg.272]    [Pg.275]    [Pg.277]    [Pg.280]    [Pg.281]    [Pg.282]    [Pg.282]    [Pg.283]    [Pg.285]    [Pg.287]   
See also in sourсe #XX -- [ Pg.681 ]




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