加熱が大豆蛋白質に及ぼす影響

概要

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Effects of heating on soybean meal proteins were examinded by means of gel-filtration on Sephadex G-200, acryl amide gel electrophoresis and observation under electron microscope. Whole water extract, acid-precipitated protein and calcium-precipitated protein solutions were prepared and submitted to gel-filtration and acryl amide gel electrophoresis. In the case of Sephadex column chromatography, whole water extract was separated into five fractions, being estimated by 280mμ absorption. In chromatograms of acid-or calciumprecipitated protein, the later eluted fractions decreased or almost disappeared. By heating of these solutions including whole water extract, the fractions except the first eluted main fraction were much reduced or disappeared, perhaps transferring to the first one by association. On acryl amide gel electrophoretical patterns, it was recognized that some fast-moving bands faded away after heating. By electron microscopy of whole water extract in the presence of calcium chloride, numerous spheres of about 0.05μ were observed scattering all over the field. The spheres aggregated randomly to irregular blocks by heating. It seems to be concluded that heating soybean protein solutions at 100°C for 15 min gives the trend to associate as previously indicated by ultracentrifugation analysis.
社団法人日本農芸化学会の論文