Cereal Chem 50:417 - 427.  |  VIEW ARTICLE
The Modification of Wheat Flour Proteins with Succinic Anhydride.

D. R. Grant. Copyright 1973 by the American Association of Cereal Chemists, Inc. 

Treatment of wheat flour with succinic anhydride in aqueous dioxane suspension results in the conversion of 95% of the protein to derivatives soluble in water. Decreasing the pH below 5.0 results in precipitation of most of these derivatives. A substantial fraction was precipitated at 1% Na2SO4 concentration, but another fraction was insensitive to high salt concentrations. Sensitivity to low pH and salt concentration diminished as the dioxane content of the system increased. G-100 Sephadex chromatography and viscosity studies indicated that the succinylated derivatives are more extensively dissociated in solution than untreated flour proteins in a dilute acetic acid extract. Polyacrylamide gel electrophoresis and ultracentrifugal analysis indicated that some association phenomena still occur unless the derivatives are dissolved in concentrated urea solutions. Gel electrophoresis of native and succinylated solutions of serum albumin, pepsin, and lysozyme indicated that the succinylation of a single protein species is likely to produce a heterogeneous product.