Differential recovery of lupin proteins from the gluten matrix in lupin–wheat bread as revealed by mass spectrometry and two-dimensional electrophoresis
Islam, S., Ma, W., Yan, G., Gao, L. and Appels, R. (2011) Differential recovery of lupin proteins from the gluten matrix in lupin–wheat bread as revealed by mass spectrometry and two-dimensional electrophoresis. Journal of Agricultural and Food Chemistry, 59 (12). pp. 6696-6704.
*Subscription may be required
Bread made from a mixture of wheat and lupin flour possesses a number of health benefits. The addition of lupin flour to wheat flour during breadmaking has major effects on bread properties. The present study investigated the lupin and wheat flour protein interactions during the breadmaking process including dough formation and baking by using proteomics research technologies including MS/MS to identify the proteins. Results revealed that qualitatively most proteins from both lupin and wheat flour remained unchanged after baking as per electrophoretic behavior, whereas some were incorporated into the bread gluten matrix and became unextractable. Most of the lupin alpha-conglutins could be readily extracted from the lupin wheat bread even at low salt and nonreducing/nondenaturing extraction conditions. In contrast, most of the beta-conglutins lost extractability, suggesting that they were trapped in the bread gluten matrix. The higher thermal stability of alpha-conglutins compared to beta-conglutins is speculated to account for this difference.
|Publication Type:||Journal Article|
|Murdoch Affiliation:||Centre for Comparative Genomics|
Western Australian State Agricultural Biotechnology Centre
|Publisher:||American Chemical Society|
|Copyright:||© 2011 American Chemical Society|
|Item Control Page|