Cereal Chem. 73 (4):490-494 |
Modifications of Wheat Proteins Due to Flour Chlorination.
M. P. Duviau (1), H. Yamamoto (2,3), P. K. W. Ng (2), and K. Kobrehel (1,4). (1) Laboratoire de Biochimie et Biologie Moléculaire des Céréales, INRA, 2, Place Viala 34060 Montpellier-Cedex, France. (2) Department of Food Science and Human Nutrition, Michigan State University, East Lansing, MI 48824. (3) Present address: Yamazaki Baking Co., Ltd., 3-15-6, Chitose, Sumida-ku, Tokyo, 130, Japan. (4) Corresponding author. E-mail: <Kobrehel@ENSAM.inra.fr> Accepted March 28, 1996. Copyright 1996 by the American Association of Cereal Chemists, Inc.
The extractability of wheat flour proteins underwent considerable changes as the result of chlorination, especially as detected under different conditions for sequential protein extraction. Compared to controls, changes in protein extractability were greater when flours were chlorinated to pH 4.3 than to pH 4.8. Gliadins seemed to be more affected than glutenins. Low molecular weight proteins, whose molecular mass ranged between 9 and 15 kDa, were also considerably affected, but to a varying extent. While free -SH groups decreased slightly in treated samples, results suggested that SS bonds did not seem to be affected under chlorination, and their accessibility to thioredoxin and to dithiothreitol also remained unchanged.