Journal
PLOS ONE
Volume 9, Issue 6, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0096914
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Funding
- Intelligent Synthetic Biology Center of Global Frontier Project - Ministry of Education, Science and Technology of Republic of Korea [2011-0031967]
- China Major Projects [2012ZX09503001-003]
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The ginsenoside Rg(2)(S), which is one of the pharmaceutical components of ginseng, is known to have neuroprotective, antiinflammation, and anti-diabetic effects. However, the usage of ginsenoside Rg2(S) is restricted owing to the small amounts found in white and red ginseng. To enhance the production of ginsenoside Rg2(S) as a 100 gram unit with high specificity, yield, and purity, an enzymatic bioconversion method was developed to adopt the recombinant glycoside hydrolase (BglPC28), which is a ginsenoside-transforming recombinant beta-glucosidase from Pseudonocardia sp. strain Gsoil 1536. The gene, termed bglPC28, encoding beta-glucosidase (BglPC28) belonging to the glycoside hydrolase family 3 was cloned. bglPC28 consists of 2,232 bp (743 amino acid residues) with a predicted molecular mass of 78,975 Da. This enzyme was overexpressed in Escherichia coli BL21(DE3) using a GST-fused pGEX 4T-1 vector system. The optimum conditions of the recombinant BglPC28 were pH 7.0 and 37 degrees C. BglPC28 can effectively transform the ginsenoside Re to Rg2(S); the Km values of PNPG and Re were 6.36 +/- 1.10 and 1.42 +/- 0.13 mM, respectively, and the V-max values were 40.0 +/- 2.55 and 5.62 +/- 0.21 mmol min(-1) mg(-)1 of protein, respectively. A scaled-up biotransformation reaction was performed in a 10 L jar fermenter at pH 7.0 and 30 degrees C for 12 hours with a concentration of 20 mg/ml of ginsenoside Re from American ginseng roots. Finally, 113 g of Rg2(S) was produced from 150 g of Re with 84.0 +/- 1.1% chromatographic purity. These results suggest that this enzymatic method could be usefully exploited in the preparation of ginsenoside Rg(2)(S) in the cosmetics, functional food, and pharmaceutical industries.
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