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Viscosity glutenin

Gliadins, unlike glutenins, contribute to the viscosity and the extensibility of the gluten and not its strength. [Pg.31]

Enzymic actions that depolymerise proteins such as the high molecular weight glutenins will cause the viscosity of the dough to drop. This outcome is predictable on the basis of polymer science. [Pg.32]

Relative to secondary structure, viscosity, sedimentation velocity, ultraviolet difference spectra and optical rotatory dispersion studies (4,24,25) showed that glutenin appears to be an assymetric molecule with a low a-helix content (10-15%). Glutenin contained more a-helix structure in hydrochloric acid solutions and less in urea solutions. The amount of a-helix structure is also influenced by changes in ionic strength (26). [Pg.198]

Taylor N.W. and Cluskey, J.E. Wheat gluten and its glutenin component Viscosity, diffusion and sedimentation studies. Am/i. Biochem. Biophys. 97 399-405, 1962. [Pg.97]


See other pages where Viscosity glutenin is mentioned: [Pg.120]    [Pg.120]    [Pg.121]    [Pg.155]    [Pg.202]    [Pg.486]    [Pg.155]    [Pg.380]    [Pg.381]    [Pg.70]    [Pg.693]   
See also in sourсe #XX -- [ Pg.120 ]

See also in sourсe #XX -- [ Pg.36 , Pg.41 , Pg.42 ]




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