title: Characterization of a β-glucosidase from Sulfolobus solfataricus for isoflavone glycosides.
abstract: The specific activity of a recombinant β-glucosidase from Sulfolobus solfataricus for isoflavones was: daidzin > glycitin > genistin > malonyl genistin > malonyl daidzin > malonyl glycitin. The hydrolytic activity of this enzyme for daidzin was highest at pH 5.5 and 90°C with a half-life of 18 h, a K (m) of 0.5 mM, and a k (cat) of 2532 s(-1). The enzyme converted 1 mM daidzin to 1 mM daidzein after 1 h with a molar yield of 100% and a productivity of 1 mM h(-1). Among β-glucosidases, that from S. solfataricus β had the highest thermostability, k (cat), k (cat)/K (m), conversion yield, and productivity in the hydrolysis of daidzin.
authors: Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul, 143-701, Republic of Korea.
authors: Bi-Na
authors: BN
authors: Kim
authors: Soo-Jin
authors: SJ
authors: Yeom
authors: Yeong-Su
authors: YS
authors: Kim
authors: Deok-Kun
authors: DK
authors: Oh
mesh_terms: D004795:Enzyme Stability; D006027:Glycosides / Q000378:metabolism*; D006207:Half-Life; D006863:Hydrogen-Ion Concentration; D007529:Isoflavones / Q000378:metabolism*; D007700:Kinetics; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D013696:Temperature; D001617:beta-Glucosidase / Q000378:metabolism*
chemical_list: D006027:Glycosides; D007529:Isoflavones; D011994:Recombinant Proteins; D001617:beta-Glucosidase