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Biotransformation of Protopanaxadiol-Type Ginsenosides in Korean Ginseng Extract into Food-Available Compound K by an Extracellular Enzyme from Aspergillus niger
Author(s) -
Eun-Bi Jeong,
Se-A Kim,
KyungChul Shin,
DeokKun Oh
Publication year - 2020
Publication title -
journal of microbiology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 64
eISSN - 1738-8872
pISSN - 1017-7825
DOI - 10.4014/jmb.2007.07003
Subject(s) - protopanaxadiol , ginseng , biotransformation , ginsenoside , chemistry , aspergillus niger , araliaceae , sapogenin , traditional medicine , dammarane , biochemistry , glycoside , enzyme , triterpene , stereochemistry , medicine , alternative medicine , pathology
Compound K (C-K) is one of the most pharmaceutically effective ginsenosides, but it is absent in natural ginseng. However, C-K can be obtained through the hydrolysis of protopanaxadiol-type ginsenosides (PPDGs) in natural ginseng. The aim of this study was to obtain the high concentration of food-available C-K using PPDGs in Korean ginseng extract by an extracellular enzyme from Aspergillus niger KACC 46495. A. niger was cultivated in the culture medium containing the inducer carboxymethyl cellulose (CMC) for 6 days. The extracellular enzyme extracted from A. niger was prepared from the culture broth by filtration, ammonium sulfate, and dialysis. The extracellular enzyme was used for C-K production using PPDGs. The glycoside-hydrolyzing pathways for converting PPDGs into C-K by the extracellular enzyme were Rb1 → Rd → F2 → C-K, Rb2 → Rd or compound O → F2 or compound Y → C-K, and Rc → Rd or compound Mc1 → F2 or compound Mc → C-K. The extracellular enzyme from A. niger at 8.0 mg/ml, which was obtained by the induction of CMC during the cultivation, converted 6.0 mg/ml (5.6 mM) PPDGs in Korean ginseng extract into 2.8 mg/ml (4.5 mM) food-available C-K in 9 h, with a productivity of 313 mg/l/h and a molar conversion of 80%. To the best of our knowledge, the productivity and concentration of C-K of the extracellular enzyme are the highest among those by crude enzymes from wild-type microorganisms.

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