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Characterization of a Novel Ginsenoside MT1 Produced by an Enzymatic Transrhamnosylation of Protopanaxatriol-Type Ginsenosides Re.


ABSTRACT: BACKGROUND:Ginsenosides, triterpene saponins of Panax species, are considered the main active ingredients responsible for various pharmacological activities. Herein, a new protopanaxatriol-type ginsenoside called "ginsenoside MT1" is described; it was accidentally found among the enzymatic conversion products of ginsenoside Re. METHOD:We analyzed the conversion mechanism and found that recombinant ?-glucosidase (MT619) transglycosylated the outer rhamnopyranoside of Re at the C-6 position to glucopyranoside at C-20. The production of MT1 by trans-rhamnosylation was optimized and pure MT1 was obtained through various chromatographic processes. RESULTS:The structure of MT1 was elucidated based on spectral data: (20S)-3?,6?,12?,20-tetrahydroxydammarene-20-O-[?-L-rhamnopyranosyl(1?2)-?-D-glucopyranoside]. This dammarane-type triterpene saponin was confirmed as a novel compound. CONCLUSION:Based on the functions of ginsenosides with similar structures, we believe that this ginsenoside MT1 may have great potential in the development of nutraceutical, pharmaceutical or cosmeceutical products.

SUBMITTER: Jeon BM 

PROVIDER: S-EPMC7226242 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Characterization of a Novel Ginsenoside MT1 Produced by an Enzymatic Transrhamnosylation of Protopanaxatriol-Type Ginsenosides Re.

Jeon Byeong-Min BM   Baek Jong-In JI   Kim Min-Sung MS   Kim Sun-Chang SC   Cui Chang-Hao CH  

Biomolecules 20200331 4


<h4>Background</h4>Ginsenosides, triterpene saponins of <i>Panax</i> species, are considered the main active ingredients responsible for various pharmacological activities. Herein, a new protopanaxatriol-type ginsenoside called "ginsenoside MT1" is described; it was accidentally found among the enzymatic conversion products of ginsenoside Re.<h4>Method</h4>We analyzed the conversion mechanism and found that recombinant β-glucosidase (MT619) transglycosylated the outer rhamnopyranoside of Re at t  ...[more]

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