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Highly selective hydrolysis for the outer glucose at the C-20 position in ginsenosides by β-glucosidase from Thermus thermophilus and its application to the production of ginsenoside F2 from gypenoside XVII

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Abstract

β-Glucosidase from Thermus thermophilus has specific hydrolytic activity for the outer glucose at the C-20 position in protopanaxadiol-type ginsenosides without hydrolysis of the inner glucose. The hydrolytic activity of the enzyme for gypenoside XVII was optimal at pH 6.5 and 90 °C, with a half-life of 1 h with 3 g enzyme l−1 and 4 g gypenoside XVII l−1. Under the optimized conditions, the enzyme converted the substrate gypenoside XVII to ginsenoside F2 with a molar yield of 100 % and a productivity of 4 g l−1 h−1. The conversion yield and productivity of ginsenoside F2 are the highest reported thus far among enzymatic transformations.

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Acknowledgments

This work was supported by the Basic Research Lab Program (No. 2010-0019306), the National Research Foundation, the Ministry of Education, Science and Technology, Republic of Korea.

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Correspondence to Deok-Kun Oh.

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Shin, KC., Seo, MJ., Oh, HJ. et al. Highly selective hydrolysis for the outer glucose at the C-20 position in ginsenosides by β-glucosidase from Thermus thermophilus and its application to the production of ginsenoside F2 from gypenoside XVII. Biotechnol Lett 36, 1287–1293 (2014). https://doi.org/10.1007/s10529-014-1472-y

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  • DOI: https://doi.org/10.1007/s10529-014-1472-y

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