52705-93-8Relevant articles and documents
A novel ginsenoside-hydrolyzing enzyme from Penicillium oxalicum and its application in ginsenoside Rd production
Gao, Juan,Hu, Yanbo,Ji, Li,Wang, Nan,Wang, Jiao,Tai, Guihua,Zhou, Yifa
, p. 305 - 312 (2013)
The fungus Penicillum oxalicum can selectively metabolize the major 20(S)-protopanaxadiol ginsenosides Rb1, Rb2, and Rc using extracellular glycosidases yielding a series of bioactive metabolites. A β-glucosidase GH1 was purified from the culture of P. oxalicum with a yield of 9.5% and a specific activity of 3.9 × 103 U/mg. GH1 was a tetramer with a native molecular weight of 484 kDa and its pI value was pH 4.2. GH1 specifically cleaved the β-(1-6)-glucosidic linkage at C-20 site of ginsenoside Rb1 to give the sole product Rd. The optimum conditions were established to be pH 4.5, 55°C, and 0.25 U/ml purified enzyme at 2 mg/ml ginsenoside Rb1. GH1 could be used in the pharmaceutical industry.
Biotransformation of the principal ginsenosides of Panax ginseng into minor glycosides through the action of bacterium Paenibacillus sp. BG134
Ten,Chae,Yoo
, (2014)
The bacterium Paenibacillus sp. BG134 was capable of biotransforming the principal 20(S)-protopanaxadiol ginsenosides Rc, Rb2, Rd, and Rb1 into the corresponding minor glycosides C-Mc1, C-O, and F-2. The specificity of Paenibacillus
Rational design of a β-glycosidase with high regiospecificity for triterpenoid tailoring
Park, Sang Jin,Choi, Jung Min,Kyeong, Hyun-Ho,Kim, Song-Gun,Kim, Hak-Sung
, p. 854 - 860 (2015/03/30)
Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β-glycosidase with high regiospecificity for triterpenoids. A β-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 ? resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity.
