作者: ROBIN Y.-Y. CHIOU
DOI: 10.1111/J.1745-4514.1990.TB00835.X
关键词: Cystine 、 Chromatography 、 Freeze-drying 、 Electrophoresis 、 Chemistry 、 Nitrogen 、 Roasting 、 Methionine 、 Globulin 、 Lysine
摘要: Arachin and conarachin were purified from phosphate buffer (0.20 0.05 M, pH 7.9) extracts using ammonium sulfate fractionation at 40 60–85% saturation, respectively. Characterization on SDS-PAGE gel revealed that arachin was composed of five major subunits whereas consisted one subunit. Methionine, lysine, 1/2 cystine content was, respectively, about three-, two- two-fold higher than in arachin. During dry roasting whole peanut kernels lyophilization 150°C for 60 min, the nitrogen soluble indexes decreased with time. Changes comparatively those When buffered subjected to boiling water bath cooking native protein patterns conarachin, as shown gradient PAGE, varied significantly heating Subunits detected did not qualitatively vary.