Characteristics of protein profile of low allergenic rice variety, "Yukihikari"
2005
Momma, M.(National Food Research Inst, Tsukuba, Ibaraki (Japan))
Protein profile of refined rice grain including low-allergenic variety, "Yukihikari", was analyzed by two-dimensional electrophoresis and mBBr fluorescence labeling. No significant difference in salt-soluble protein composition was observed among the three varieties. SDS-PAGE pattern of water-soluble proteins from Yukihikari and Kirara397 were similar while Koshihikari contained less high- molecular weight protein (25-80-kDa). Further analysis by two-dimensional electrophoresis revealed that water soluble protein fraction of Yukihikari contained higher amount of 32-kDa and 70-90-kDa polypeptides and less of 28,25, and 20 -kDa polypeptides comparing to Kirara397. In the result of fluorescence labeling test, disulfide bonds in two major allergen proteins of rice, alpha-globulin and alpha-amylase inhibitor were found to be resistant to chemical or enzymatic moderate reduction. Content of these disulfide proteins dissolved in water-soluble fraction were lower in the two varieties from Hokkaido area, Yukihikari and Kirara397 than Koshihikari. These results implied the solubility of disulfide allergens in refined rice grains were different among the rice varieties.
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