Evidence map›Paper›PMID 25838236›Full record

ArticleJournal of industrial microbiology & biotechnology2015

Overexpression and characterization of a Ca(2+) activated thermostable β-glucosidase with high ginsenoside Rb1 to ginsenoside 20(S)-Rg3 bioconversion productivity.

Jingcong Xie, Dongxia Zhao, Linguo Zhao, Jianjun Pei, Wei Xiao, Gang Ding, Zhenzhong Wang

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Article in Journal of industrial microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. Efficient Biosynthesis of Gastrodin by UDP-Glycosyltransferase fromJournal of microbiology and biotechnology · 2025
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  13. Immobilization of GH78 α-L-Rhamnosidase fromJournal of microbiology and biotechnology · 2021
    Article
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  15. Article
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  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Jingcong XieCollege of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing, 210037, China.
Dongxia Zhao
Linguo Zhao
Jianjun Pei
Wei Xiao
Gang Ding
Zhenzhong Wang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The thermostable β-glucosidase gene from Thermotoga petrophila DSM 13995 was cloned and overexpressed in Escherichia coli. The activity of the recombinant β-glucosidase was 21 U/mL in the LB medium. Recombinant β-glucosidase was purified, and its molecular weight was approximately 81 kDa. The optimal activity was at pH 5.0 and 90 °C, and the thermostability of the enzyme was improved by Ca(2+). The β-glucosidase had high selectivity for cleaving the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1, which produced the pharmacologically active minor ginsenoside 20(S)-Rg3. In a reaction at 90 °C and pH 5.0, 10 g/L of ginsenoside Rb1 was transformed into 6.93 g/L of Rg3 within 90 min, with a corresponding molar conversion of 97.9%, and Rg3 productivity of 4620 mg/L/h. This study is the first report of a GH3-family enzyme that used Ca(2+) to improve its thermostability, and it is the first report on the high substrate concentration bioconversion of ginsenoside Rb1 to ginsenoside 20(S)-Rg3 by using thermostable β-glucosidase under high temperature.

Indexed as

beta-GlucosidaseBiotransformationCalciumEnzyme ActivationEnzyme StabilityEscherichia coliGinsenosidesGram-Negative Anaerobic Straight, Curved, and Helical RodsHydrogen-Ion ConcentrationMolecular WeightTemperaturebeta-GlucosidaseCalciumginsenoside Rb1Ginsenosides

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.