บทคัดย่องานวิจัย

หมวดหมู่ : ฐานข้อมูลงานวิจัย

Purification and characterization of furostanol glycoside 26-O- beta -glucosidase from Costus speciosus rhizomes.

Inoue, K.; Ebizuka, Y.;

FEBS Letters Year: 1996 Vol: 378 Issue: 2 Pages: 157-160 Ref: 26 ref.

1996

บทคัดย่อ

Purification and characterization of furostanol glycoside 26-O- beta -glucosidase from Costus speciosus rhizomes.

In plants, spirostanol glycosides (steroid saponins) are known to be formed from furostanol glycosides during postharvest treatment and storage. Furostanol glycoside 26-O- beta -glucosidase (F26G) involved in this conversion was purified to apparent homogeneity for the first time from C. speciosus rhizomes which accumulate these glycosides. The enzyme was highly specific for cleavage of the glucose moiety bound to C-26 of furostanol glycosides; Km for protogracillin was 50 micro M. Glucono-1,5-lactone (a typical beta -glucosidase inhibitor) and diosgenin (an aglycone of spirostanol glycosides) strongly inhibited the enzyme activity. Purified F26G, having native apparent MW 110 kDa, is dimeric, comprising subunits of MW 54 kDa and 58 kDa. The N-terminal sequence of the 54 kDa protein has great similarity to sequences found in the N-terminal regions of known plant beta -glucosidases.