title: Purification and characterization of ginsenoside-alpha-L-rhamnosidase.
abstract: In this paper the ginsenoside-alpha-(1-->2)-L-rhamnosidase from microorganisms was purified and characterized. The enzyme hydrolyzed the 6-C, alpha-(1-->2)-L-rhamnoside of 20(S) and 20(R)-ginsenoside Rg2 to produce the 20(S) and 20(R)-ginsenoside Rh1, but hardly hydrolyzed the alpha-rhamnoside of pNPR. The enzyme molecular weight was about 53 kDa. The optimum temperature of enzyme reaction was 40 degrees C, and the optimum pH was 5.
authors.affiliation: Department of Food Science and Biotechnology, Dalian Institute (College) of Light Industry, Ganjingzi-qu, PR China.
authors.forename: Hongshan
authors.initials: H
authors.lastname: Yu
authors.forename: Jinmei
authors.initials: J
authors.lastname: Gong
authors.forename: Chunzhi
authors.initials: C
authors.lastname: Zhang
authors.forename: Fengxie
authors.initials: F
authors.lastname: Jin
mesh_terms: D020095:Absidia / Q000201:enzymology*; D005285:Fermentation; D036145:Ginsenosides; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D012503:Saponins / Q000378:metabolism*
chemical_list: D036145:Ginsenosides; D012503:Saponins; D006026:Glycoside Hydrolases; C022525:alpha-L-rhamnosidase