Evidence map›Paper›PMID 28423055›Full record

ArticlePloS one2017

Comparative analysis of the expression level of recombinant ginsenoside-transforming β-glucosidase in GRAS hosts and mass production of the ginsenoside Rh2-Mix.

Muhammad Zubair Siddiqi, Chang-Hao Cui, Seul-Ki Park, Nam Soo Han, Sun-Chang Kim, Wan-Taek Im

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 3 institutions in 1 country.

Muhammad Zubair SiddiqiDepartment of Biotechnology, Hankyoung National University, Kyonggi-do, Republic of Korea.
Chang-Hao CuiIntelligent Synthetic Biology Center, Yuseong-gu, Daejeon, Republic of Korea.
Seul-Ki ParkIntelligent Synthetic Biology Center, Yuseong-gu, Daejeon, Republic of Korea.
Nam Soo HanBrain Korea 21 Center for Bio-Resource Development, Division of Animal, Horticultural and Food Sciences, Chungbuk National University, Cheongju, Korea.
Sun-Chang KimIntelligent Synthetic Biology Center, Yuseong-gu, Daejeon, Republic of Korea.
Wan-Taek ImDepartment of Biotechnology, Hankyoung National University, Kyonggi-do, Republic of Korea.ORCID http://orcid.org/0000-0002-0545-1279
Intelligent Synthetic Biology Center · KRHankyong National University · KRChungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ginsenoside Rh2, a pharmaceutically active component of ginseng, is known to have anticancer and antitumor effects. However, white ginseng and red ginseng have extremely low concentrations of Rh2 or Rh2-Mix [20(S)-Rh2, 20(R)-Rh2, Rk2, and Rh3]. To enhance the production of food-grade ginsenoside Rh2, an edible enzymatic bioconversion technique was developed adopting GRAS host strains. A β-glucosidase (BglPm), which has ginsenoside conversion ability, was expressed in three GRAS host strains (Corynebacterium glutamicum, Saccharomyces cerevisiae and Lactococus lactis) by using a different vector system. Enzyme activity in these three GRAS hosts were 75.4%, 11.5%, and 9.3%, respectively, compared to that in the E. coli pGEX 4T-1 expression system. The highly expressed BglPm_C in C. glutamicum can effectively transform the ginsenoside Rg3-Mix [20(S)-Rg3, 20(R)-Rg3, Rk1, Rg5] to Rh2-Mix [20(S)-Rh2, 20(R)-Rh2, Rk2, Rh3] using a scaled-up biotransformation reaction, which was performed in a 10-L jar fermenter at pH 6.5/7.0 and 37°C for 24 h. To our knowledge, this is the first report in which 50 g of PPD-Mix (Rb1, Rb2, Rb3, Rc, and Rd) as a starting substrate was converted to ginsenoside Rg3-Mix by acid heat treatment and then 24.5-g Rh2-Mix was obtained by enzymatic transformation of Rg3-Mix through by BglPm_C. Utilization of this enzymatic method adopting a GRAS host could be usefully exploited in the preparation of ginsenoside Rh2-Mix in cosmetics, functional food, and pharmaceutical industries, thereby replacing the E. coli expression system.

Indexed as

Bacterial Proteinsbeta-GlucosidaseBiotransformationCloning, MolecularCorynebacterium glutamicumEscherichia coliFungal ProteinsGene ExpressionGenetic VectorsGinsenosidesHydrogen-Ion ConcentrationIndustrial MicrobiologyKineticsLactococcus lactisMolecular WeightPanaxBacterial Proteinsbeta-GlucosidaseFungal Proteinsginsenoside-beta-glucosidaseginsenoside Rg3ginsenoside Rh2GinsenosidesRecombinant Proteins

Identifiers

PMID28423055
PMCPMC5396970
OpenAlexW2605805510

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.