Cereal Chem 61:353 - 356.  |  VIEW ARTICLE
Chemical and Physical Properties of Proteins in Wet-Milled Corn Gluten.

P. E. Neumann, J. S. Wall, and C. E. Walker. Copyright 1984 by the American Association of Cereal Chemists, Inc. 

The chemical and physical properties of proteins in wet-milled corn gluten were investigated to establish possible food uses. Commercially produced wet corn gluten (WCG) (28% protein, 60% moisture) and commercially dried corn gluten meal (DCGM) (62% protein, 10% moisture) were sequentially extracted with 0.5M NaCl and 70% ethanol, and then with 0.5% sodium dodecyl sulfate (SDS) pH 10 buffer and 0.5% SDS containing 0.6% 2-mercaptoethanol (2-ME) in pH 10 buffer of 70% ethanol containing 0.6% 2- ME and 0.5% SDS plus 0.6% 2-ME in pH 10 buffer. The yields of proteins soluble in 70% ethanol and 0.5% SDS in pH 10 buffer are much greater from gluten than from native corn, demonstrating that SO2 in the steepwater from wet milling cleaves protein disulfide bonds. Analysis for sulfhydryl and disulfide content, total cysteine-cystine compounds as cysteic acid and total sulfur showed that much of the cystine is converted to other derivatives of cysteine during steeping. In contrast to WCG, DCGM had no cysteine, indicating that sulfhydryls were oxidized during drying of gluten. Wet corn gluten (pH 3.6) and WCG adjusted to pH 7.0 form doughs when mixed at proper moisture levels, but DCGM does not.