Surface Structure of Natural Rubber Latex Particles from Electrophoretic Mobility Data

✍ Scribed by C.C. Ho; T. Kondo; N. Muramatsu; H. Ohshima

• Publisher: Elsevier Science
• Year: 1996
• Tongue: English
• Weight: 76 KB
• Volume: 178
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1996.0139

✦ Synopsis

soaps, hydrolysis products of phospholipids (2, 3). The role Fresh natural rubber latex particles are stabilized by adsorbed of adsorbed proteins on latex stabilization is less important proteins and phospholipids while those for high-ammonia latex in latex concentrate (2). Some polypeptides from the hyconcentrate are stabilized mainly by adsorbed long-chain fatty acid drolyzed proteins could also become adsorbed at the latex soaps, the hydrolysis products of phospholipids. The structure of particle surface.

this surface layer surrounding the latex particles is analyzed using Direct elucidation of the surface structure of the rubber the electrophoresis model of Ohshima and Kondo. Good latex particles has not been successful so far because the agreement between theoretical and observed electrophoretic mobillatex is easily destabilized when its surface constituents are ity was found, except at very low ionic strength. The results were removed. Chemical modifications of the surface groupings consistent with a model of an uncharged bared polyisoprene latex

(2) followed by mobility measurements did yield some inparticle coated by a charged mixed layer of long-chain fatty acid formation on the surface. However, its structure is far from soaps, proteins, and polypeptides of finite thickness in matured latex concentrate. This surface layer is ion-penetrable and its resis-resolved. For example, it is not clear how the long-chain tance to liquid flow changes with time on prolonged hydrolysis. fatty acid soaps and proteins are arranged at the rubber/