Cereal Chem 62:166-169   |  VIEW ARTICLE
Model Experiments on Hydrophobicity of Chlorinated Starch and Hydrophobicity of Chlorinated Surface Protein.

M. Seguchi. Copyright 1985 by the American Association of Cereal Chemists, Inc. 

Chlorination of dried glass powder or glass beads, which were coated with gelatin, imparted strong oil- binding ability similar to that of chlorinated starch. Soluble proteins such as gelatin, bovine serum albumin (BSA), or ovalbumin formed hydrophobic, water-insoluble thin film after chlorination. These films could be dissolved in weak alkali or 1% sodium dedecyl sulfate (SDS) but became insoluble when dialyzed against water. SDS disc gel electrophoresis of chlorinated BSA showed no polymerization or decomposition. Ultraviolet spectra of BSA or gelatin showed an increased absorption between 290 and 400 nm by chlorination. Paper chromatograms of chlorinated tyrosine, lysine, or cystine showed new hydrophobic derivatives. It is assumed that these derivatives rendered the hydrophobic character to the protein.