Earticle

초록

영어

The production of deglycosylated isoflavones from glycosylated isoflavones and soy extract was performed using a recombinant β- glucosidase from Pyrococcus furiosus. The activity for genistin was optimal at pH 6.0 and 95 °C with a half-life of 59 h at 95 °C. The kinetic properties Km, kcat, and kcat/Km for genistin were determined to be 0.5 mM, 6050 s-1 and 12100 mM-1 s-1. The kcat and kcat/Km of the enzyme exhibited the highest values to date. The deglycosylated isoflavones genistin, daidzin, and glycitin at 1.0 mM were completely hydrolyzed to the glycosylated isoflavones genistein, daidzein, and glycitein, respectively, after 100, 140, and 180 min, respectively, by P. furiosus β-glucosidase. The soy flour extract of 7.5% (w/v) containing 1.0 mM genistin, 0.9 mM daidzin, and 0.3 mM glycitin were absolutely converted to genistein, daidzein, and glycitein, respectively, within 120 min. The productivities of the glycosylated isoflavones in the present study are the highest ever reported among biological methods. These results suggest that the thermostable enzyme may be useful for the industrial hydrolysis of deglycosylated isoflavones.

키워드

저자

• Soo-Jin YEOM [ Dept. of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701. ]
• Bi-Na KIM [ Dept. of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701. ]
• Yeong-Su KIM [ Dept. of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701. ]
• Deok-Kun OH [ Dept. of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576