Cereal Chem 69:607-612   |  VIEW ARTICLE

Hydrophobic Properties of Reduced and Alkylated Acetic Acid-Soluble Glutenins--- Fractionation by Hydrophobic Interaction Chromatography.

E. M. Magnus and K. Khan. Copyright 1992 by the American Association of Cereal Chemists, Inc. 

The proteins from flours of 13 wheat varieties representing different wheat classes were separated by a modified Osborne fractionation procedure. The reduced and alkylated acetic acid-soluble proteins were fractionated by hydrophobic interaction chromatography using phenyl-Sepharose CL-4B. The protein content of each fraction obtained from hydrophobic interaction chromatography was quantified by absorption at 280 nm. Often, the largest proportions of the protein were eluted with aluminum lactate buffer and with aluminum lactate buffer containing 30% 2-propanol. A larger proportion of protein was eluted with aluminum lactate buffer for soft red winter and Norwegian spring wheats than for hard red spring and hard red winter wheats, indicating lower hydrophobicity of reduced and alkylated glutenin from wheats of poor baking quality. The high-molecular-weight (HMW) glutenin subunits were also eluted with aluminum lactate buffer and with aluminum lactate buffer containing 30% 2-propanol. Sodium dodecyl sulfate electrophoregrams indicated that HMW glutenin subunits 8-10 and 12 had lower surface hydrophobicities than HMW subunits 1, 2, 2*, 5, and 7.