Purification and Characterization of New Special Ginsenosidase Hydrolyzing Multi-Glycisides of Protopanaxadiol Ginsenosides, Ginsenosidase Type I

• Published in: Chemical & Pharmaceutical Bulletin Vol. 55; no. 2; pp. 231 - 235
• Main Authors: Yu, Hongshan, Zhang, Chunzhi, Lu, Mingchun, Sun, Fang, Fu, Yaoyao, Jin, Fengxie
• 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: Aspergillus fumigatus - enzymology; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; ginsenosidase type I; Ginsenosides - metabolism; Glycoside Hydrolases - isolation & purification; Glycoside Hydrolases - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Molecular Weight; multi-glycoside hydrolysis of ginsenoside; Plants, Medicinal; PPD ginsenoside; Sapogenins - metabolism; Temperature; Triterpenes - metabolism
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.55.231

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.