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ARS Home » Plains Area » Fargo, North Dakota » Edward T. Schafer Agricultural Research Center » Cereal Crops Research » Research » Publications at this Location » Publication #196975
Title: QUANTITATIVE GLUTENIN COMPOSITION FROM GEL ELECTROPHORESIS OF FLOUR MILL STREAMS AND RELATIONSHIP TO BREADMAKING QUALITY

Author
item WANG, Y - NORTH DAKOTA STATE UNIV
item KHAN, K - NORTH DAKOTA STATE UNIV
item Hareland, Gary
item NYGARD, G - NORTH DAKOTA STATE UNIV

Submitted to: Cereal Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/4/2006
Publication Date: 5/1/2006
Citation: Wang, Y.G., Khan, K., Hareland, G.A., Nygard, G. 2006. Quantitative glutenin composition from gel electrophoresis of flour mill streams and relationship to breadmaking quality. Cereal Chemistry. 83(3):293-299.

Interpretive Summary: Three samples of hard red winter wheat (var. Nekota) were milled, and six mill streams were collected from each sample. The eighteen mill streams were analyzed separately as well as recombined to form three separate patent flours. Unreduced SDS-soluble glutenins and the total reduced proteins were separated by multistacking (MS)-SDS-PAGE and SDS-PAGE, respectively. The separated proteins were quantified by densitometry. The quantity of unreduced SDS-soluble proteins was significantly different among the mill streams at the largest molecular weight polymeric glutenin and at the smaller molecular weight polymeric glutenin origins of the MS-SDS-PAGE gels. The quantities of total subunits and the ratio of high molecular weight to low molecular weight glutenin subunits in polymeric protein samples isolated in total reduced protein extracts were significantly different among mill streams. The quantities of high molecular weight and low molecular weight glutenin subunits including 2*, 7 + 9 and 5 + 10 subunits from total reduced proteins were positively and significantly correlated with bread loaf volume. The quantities of glutenin subunits from unreduced SDS-soluble proteins were positively or negatively correlated with loaf volume at the various MS-SDS-PAGE gel origins, but the levels of correlation were not significant. These results showed that the glutenin protein composition was different among the various mill streams and demonstrated that electrophoretic analysis of the proteins in these fractions is a useful tool for understanding the variation in functional properties of flour mill streams.

Technical Abstract: Three samples of Nekota (hard red winter wheat) were milled, and six mill streams were collected from each sample. The eighteen mill streams were analyzed separately as well as recombined to form three patent flours. The methods of multistacking (MS)-SDS-PAGE and SDS-PAGE were used to separate the unreduced SDS-soluble glutenins and the total reduced proteins, respectively. The separated proteins were quantified by densitometry. The quantity of unreduced SDS-soluble proteins was significantly different among the mill streams at the 4% (largest molecular weight polymeric glutenins) and at the 10% and 12% (smaller molecular weight polymeric glutenins) origins of the MS-SDS-PAGE gels. The quantities of total HMW-GS, LMW-GS, 2*, 7 + 9 and 5 + 10 subunits and the ratio of HMW-GS to LMW-GS in polymeric protein samples isolated using preparative MS-SDS-PAGE and in total reduced protein extracts were significantly different among mill streams. The quantities of HMW-GS, LMW-GS, 2*, 7 + 9 and 5 + 10 subunits from total reduced proteins were positively and significantly correlated with loaf volume. The quantities of glutenin subunits from unreduced SDS-soluble proteins were positively or negatively correlated with loaf volume at the various MS-SDS-PAGE gel origins, but the levels of correlation were not significant. These results showed that the glutenin protein composition was different among the various mill streams and demonstrated that electrophoretic analysis of the proteins in these fractions is a useful tool for understanding the variation in functional properties of flour mill streams.