By a News Reporter-Staff News Editor at Journal of Technology -- Researchers detail new data in Colloids and Interface Science. According to news reporting out of St. Petersburg, Russia, by VerticalNews editors, the research stated, "Experimental results on the dynamic dilational surface elasticity of protein solutions are analyzed and compared. Short reviews of the protein behavior at the liquid-gas interface and the dilational surface rheology precede the main sections of this work."
Our news journalists obtained a quote from the research from St. Petersburg State University, "The kinetic dependencies of the surface elasticity differ strongly for the solutions of globular and non-globular proteins. In the latter case these dependencies are similar to those for solutions of non-ionic amphiphilic polymers and have local maxima corresponding to the formation of the distal region of the surface layer (type I). In the former case the dynamic surface elasticity is much higher (>60 mN/m) and the kinetic dependencies are monotonical and similar to the data for aqueous dispersions of solid nanoparticles (type II). The addition of strong denaturants to solutions of bovine serum albumin and beta-lactoglobulin results in an abrupt transition from the type II to type I dependencies if the denaturant concentration exceeds a certain critical value. These results give a strong argument in favor of the preservation of the protein globular structure in the course of adsorption without any denaturants. The addition of cationic surfactants also can lead to the non-monotonical kinetic dependencies of the dynamic surface elasticity indicating destruction of the protein tertiary and secondary structures. The addition of anionic surfactants gives similar results only for the protein solutions of high ionic strength. The influence of cationic surfactants on the local maxima of the kinetic dependencies of the dynamic surface elasticity for solutions of a non-globular protein (beta-casein) differs from the influence of anionic surfactants due to the heterogeneity of the charge distribution along the protein chain. In this case one can use small admixtures of ionic surfactants as probes of the adsorption mechanism."
According to the news editors, the research concluded: "The effect of polyelectrolytes on the kinetic dependencies of the dynamic surface elasticity of protein solutions is weaker than the effect of conventional surfactants but exceeds the error limits."
For more information on this research see: Protein conformational transitions at the liquid-gas interface as studied by dilational surface rheology. Advances in Colloid and Interface Science, 2014;206():222-238. Advances in Colloid and Interface Science can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Advances in Colloid and Interface Science - www.elsevier.com/wps/product/cws_home/500842)
Our news journalists report that additional information may be obtained by contacting B.A. Noskov, St. Petersburg State University, Dept. of Colloid Chem, St Petersburg 198904, Russia.
Keywords for this news article include: Russia, Eurasia, St. Petersburg, Colloids and Interface Science
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