Biotransformation of ginsenoside Rb1 to Gyp-XVII and minor ginsenoside Rg3 by endophytic bacterium Flavobacterium sp. GE 32 isolated from Panax ginseng

2019 ◽  
Vol 68 (2) ◽  
pp. 134-141 ◽  
Author(s):  
Y. Fu
Keyword(s):  
Panax Ginseng ◽  
Endophytic Bacterium ◽  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3 ◽  
Minor Ginsenoside

scholarly journals Optimum Conversion of Major Ginsenoside Rb1 to Minor Ginsenoside Rg3(S) by Pulsed Electric Field-Assisted Acid Hydrolysis Treatment

2018 ◽  
Vol 16 (1) ◽  
pp. 283-290 ◽  
Author(s):  
Chengwen Lu ◽  
Yongguang Yin
Keyword(s):  
Electric Field ◽  
Acid Hydrolysis ◽  
Conversion Rate ◽  
Pulsed Electric Field ◽  
Pulse Number ◽  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3 ◽  
Optimum Parameters ◽  
Bioactive Component ◽  
Minor Ginsenoside

AbstractGinsenoside Rg3(S) is a primary bioactive component in ginseng, which has pharmacological effects and nutritional activities. In the present study, pulsed electric field (PEF)-assisted acid hydrolysis processing was used to convert major ginsenoside Rb1 to minor ginsenoside Rg3(S). The optimum parameters of PEF assisted acid hydrolysis were analyzed by response surface methodology (RSM). The optimum processing conditions were: electric field intensity, 20 kVcm−1; acid concentration, 0.25 mol/L; pulse number, 10. The conversion rate of ginsenoside Rg3(S) achieved 68.58%, in accordance to the predicted value. The structure of hydrolyzed product was confirmed by 13C-NMR. The results suggested that PEF-assisted acid hydrolysis significantly enhanced conversion rate of ginsenoside Rg3(S).

scholarly journals Exploration and Characterization of Novel Glycoside Hydrolases from the Whole Genome of Lactobacillus ginsenosidimutans and Enriched Production of Minor Ginsenoside Rg3(S) by a Recombinant Enzymatic Process

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 288 ◽  
Author(s):  
Muhammad Zubair Siddiqi ◽  
Sathiyaraj Srinivasan ◽  
Hye Yoon Park ◽  
Wan-Taek Im
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolases ◽  
Vector System ◽  
Whole Genome ◽  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3 ◽  
Food Grade ◽  
Minor Ginsenoside ◽  
Pharmaceutical Industries ◽  
Pharmacologically Active

Background: Several studies have reported that ginsenoside Rg3(S) is effective in treating metastatic diseases, obesity, and various cancers, however, its presence in white ginseng cannot be estimated, and only a limited amount is present in red ginseng. Therefore, the use of recombinant glycosidases from a Generally Recognized As Safe (GRAS) host strain is a promising approach to enhance production of Rg3(S), which may improve nutritional activity, human health, and quality of life. Method: Lactobacillus ginsenosidimutans EMML 3041T, which was isolated from Korean fermented pickle (kimchi), presents ginsenoside-converting abilities. The strain was used to enrich the production of Rg3(S) by fermenting protopanaxadiol (PPD)-mix-type major ginsenosides (Rb1, Rb2, Rc, and Rd) in four different types of food-grade media (1, MRS; 2, Basel Food-Grade medium; 3, Basel Food-Grade medium-I, and 4, Basel Food-Grade medium-II). Due to its tendency to produce Rg3(S), the presence of glycoside hydrolase in Lactobacillus ginsenosidimutans was proposed, the whole genome was sequenced, and the probable glycoside hydrolase gene for ginsenoside conversion was cloned. Results: The L. ginsenosidimutans EMML 3041T strain was whole genome sequenced to identify the target genes. After genome sequencing, 12 sets of glycoside hydrolases were identified, of which seven sets (α,β-glucosidase and α,β-galactosidase) were cloned in Escherichia coli BL21 (DE3) using the pGEX4T-1 vector system. Among the sets of clones, only one clone (BglL.gin-952) showed ginsenoside-transforming abilities. The recombinant BglL.gin-952 comprised 952 amino acid residues and belonged to glycoside hydrolase family 3. The enzyme exhibited optimal activity at 55 °C and a pH of 7.5 and showed a promising conversion ability of major ginsenoside Rb1→Rd→Rg3(S). The recombinant enzyme (GST-BglL.gin-952) was used to mass produce Rg3(S) from major ginsenoside Rb1. Scale-up of production using 50 g of Rb1 resulted in 30 g of Rg3(S) with 74.3% chromatography purity. Conclusion: Our preliminary data demonstrated that this enzyme would be beneficial in the preparation of pharmacologically active minor ginsenoside Rg3(S) in the functional food and pharmaceutical industries.

Ginsenoside Rb1, A Major Saponin from Panax ginseng, Exerts Protective Effects Against Acetaminophen-Induced Hepatotoxicity in Mice

2019 ◽  
Vol 47 (08) ◽  
pp. 1815-1831 ◽  
Author(s):  
Shen Ren ◽  
Jing Leng ◽  
Xing-Yue Xu ◽  
Shuang Jiang ◽  
Ying-Ping Wang ◽  
...  
Keyword(s):  
Liver Injury ◽  
Panax Ginseng ◽  
Inflammatory Responses ◽  
Interleukin 1 ◽  
Protective Effects ◽  
Ginsenoside Rb1 ◽  
Drug Induced ◽  
Drug Induced Liver Injury ◽  
Oxide Synthase

Acute liver injury (ALI) induced by acetaminophen (APAP) is the main cause of drug-induced liver injury. Previous reports indicated liver failure could be alleviated by saponins (ginsenosides) from Panax ginseng against APAP-induced inflammatory responses in vivo. However, validation towards ginsenoside Rb1 as a major and marker saponin may protect liver from APAP-induced ALI and its mechanisms are poorly elucidated. In this study, the protective effects and the latent mechanisms of Rb1 action against APAP-induced hepatotoxicity were investigated. Rb1 was administered orally with 10[Formula: see text]mg/kg and 20[Formula: see text]mg/kg daily for 1 week before a single injection of APAP (250[Formula: see text]mg/kg, i.p.) 1[Formula: see text]h after the last treatment of Rb1. Serum alanine/aspartate aminotransferases (ALT/AST), liver glutathione (GSH) depletion, as well as the inflammatory cytokines, such as tumor necrosis factor-[Formula: see text] (TNF-[Formula: see text]), interleukin-1[Formula: see text] (IL-1[Formula: see text]), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2), were analyzed to indicate the underlying protective effects of Rb1 against APAP-induced hepatotoxicity with significant inflammatory responses. Histological examination further proved Rb1’s protective effects. Importantly, Rb1 mitigated the changes in the phosphorylation of MAPK and PI3K/Akt, as well as its downstream factor NF-[Formula: see text]B. In conclusion, experimental data clearly demonstrated that Rb1 exhibited a remarkable liver protective effect against APAP-induced ALI, partly through regulating MAPK and PI3K/Akt signaling pathways-mediated inflammatory responses.

Conversion of major ginsenoside Rb1 to 20(S)-ginsenoside Rg3 by Microbacterium sp. GS514

2008 ◽  
Vol 69 (1) ◽  
pp. 218-224 ◽  
Author(s):  
Le-Qin Cheng ◽  
Ju Ryun Na ◽  
Myun Ho Bang ◽  
Myung Kyum Kim ◽  
Deok-Chun Yang
Keyword(s):  
Ginsenoside Rb1 ◽  
Ginsenoside Rg3

scholarly journals Complete Genome Sequence of the Endophytic Bacterium Bacillus cereus PgBE311, Isolated from Panax ginseng

2018 ◽  
Vol 7 (21) ◽  
Author(s):  
Chi Eun Hong ◽  
Jang Uk Kim ◽  
Jung Woo Lee ◽  
Kyong Hwan Bang ◽  
Ick-Hyun Jo
Keyword(s):  
Bacillus Cereus ◽  
Panax Ginseng ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Fungal Pathogens ◽  
Endophytic Bacterium ◽  
Content Type ◽  
Cylindrocarpon Destructans ◽  
Bacterium Bacillus

Bacillus cereus PgBE311, isolated from the root tissue of a 5-year-old Panax ginseng plant, showed activities against the fungal pathogens Cylindrocarpon destructans and Botrytis cinerea. Here, we report the genome sequence of B. cereus PgBE311.

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