The recombinant thermostable β-glucosidase from Thermotoga thermarum DSM 5069T exhibited high selectivity to catalyze the conversion of ginsenoside Re and Rg1 to the more pharmacologically active minor ginsenoside Rg2 and Rh1, respectively. At a concentration of 1.36 U/mL of the enzyme, a temperature of 85°C, and pH 5.5, 10 g/L ginsenoside Re was transformed into 8.02 g/L Rg2 within 60 min, and 2 g/L ginsenoside Rg1 was transformed into 1.56 g/L Rh1 within 60 min. This paper provides the first report on the production of ginsenoside Rg2 and Rh1 by a highly thermostable β-glucosidase.
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Acknowledgment
This work was supported by the Natural Science Foundation of Jiangsu Province of China (Grant No. BK20131423), the Open Fund of Jiangsu Key Laboratory of Biomass Based Green Fuels and Chemicals (JSBGFC12003), Postdoctoral Science Foundation of Jiangsu Province (1302022B), and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).
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Published in Khimiya Prirodnykh Soedinenii, No. 3, May–June, 2017, pp. 402–405.
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Pei, J., Wu, T., Yao, T. et al. Biotransformation of Ginsenosides Re and Rg1 into Rg2 and Rh1 by Thermostable β-Glucosidase from Thermotoga thermarum . Chem Nat Compd 53, 472–477 (2017). https://doi.org/10.1007/s10600-017-2025-0
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DOI: https://doi.org/10.1007/s10600-017-2025-0