期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 58, 期 15, 页码 8872-8878出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf101848x
关键词
beta-Glucosidase; okara; dithiothreltol; soybean Isoflavones
A novel beta-glucosidase was isolated from soybean okara in this study. Along with the beta-glucosidase, a considerable basic 7S globulin of soybean was obtained in the initial extraction products. The protein samples pretreated with 130 mM dithiothreitol before the step of CM-Sepharose chromatography could greatly enhance the separation of the targeted beta-glucosidase from the impurities. The purified beta-glucosidase was found to be a monomer estimated to be 75 kDa by SDS-PAGE. The optimal temperature and pH for this beta-glucosidase were 45 degrees C and 4.5, respectively. The activity of this purified beta-glucosidase was completely inhibited by 1 mM Hg2+ or 10 mM Al3+ ion, and glucose and mannose also affected the activity. This beta-glucosidase possessed strict specificity toward glucosyl isoflavones but not malonylglucosidic conjugates of isoflavones of soybean. The N-terminal amino acid sequence of the j3-glucosidase was EYLKYKDPKA-, which highly matched that of glycosidases in maize (Zea mays) and wheat (Triticum asetivum).
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