Highly selective hydrolysis for the outer glucose at the C-20 position in ginsenosides by beta-glucosidase from Thermus thermophilus and its application to the production of ginsenoside F-2 from gypenoside XVII

作者：Shin Kyung Chul; Seo Min Ju; Oh Hye Jin; Oh Deok Kun^*

来源：Biotechnology Letters, 2014, 36(6): 1287-1293.

DOI：10.1007/s10529-014-1472-y

• Biotransformation
• Ginsenoside F-2
• beta-Glucosidase
• Gypenoside
• Substrate specificity
• Thermostable beta-glucosidase
• Thermus thermophilus

beta-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 A degrees 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 F-2 with a molar yield of 100 % and a productivity of 4 g l(-1) h(-1). The conversion yield and productivity of ginsenoside F-2 are the highest reported thus far among enzymatic transformations.

• 出版日期2014-6