Purification and Characterization of New Special Ginsenosidase Hydrolyzing Multi-Glycisides of Protopanaxadiol Ginsenosides, Ginsenosidase Type I
In this paper, the new type ginsenosidase which hydrolyzing multi-glycosides of ginsenoside, named ginsenoside type I from Aspergillus sp.g48p strain was isolated, characterized and generally described. The enzyme molecular weight was about 80 kDa. Ginsenosidase type I can hydrolyze different glycos...
Saved in:
Published in | Chemical & Pharmaceutical Bulletin Vol. 55; no. 2; pp. 231 - 235 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English Japanese |
Published |
Japan
The Pharmaceutical Society of Japan
01.02.2007
Pharmaceutical Society of Japan Japan Science and Technology Agency |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | In this paper, the new type ginsenosidase which hydrolyzing multi-glycosides of ginsenoside, named ginsenoside type I from Aspergillus sp.g48p strain was isolated, characterized and generally described. The enzyme molecular weight was about 80 kDa. Ginsenosidase type I can hydrolyze different glycoside of protopanaxadiol type ginsenosides (PPD); i.e., can hydrolyze the 3(carbon)-O-β-glucoside of Rb1, Rb2, Rb3, Rc, Rd; can hydrolyze 20(carbon)-O-β-glucoside of Rb1, 20-O-β-xyloside of Rb3, 20-O-α-arabinoside(p) of Rb2 and 20-O-α-arabinoside(f) of Rc to produce mainly F2, compound-K (C-K) and small Rh2, but can not hydrolyze the glycosides of protopanaxatriol type ginsenoside (PPT) such as Re, Rf, Rg1. So, when the ginsenosidase type I hydrolyzed ginsenosides, the enzyme selected ginsenoside-aglycone type, can hydrolyze different glycosides of PPD type ginsenoside; however no selected glycoside type, can hydrolyze multi-glycosides of PPD type ginsenosides. These properties were novel properties, and differentiated with the other previously described glycosidases. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0009-2363 1347-5223 |
DOI: | 10.1248/cpb.55.231 |