Evidence map›Paper›PMID 38573330›Full record

ArticleApplied microbiology and biotechnology2024

Novel glycosidase from Paenibacillus lactis 154 hydrolyzing the 28-O-β-D-glucopyranosyl ester bond of oleanane-type saponins.

Zongzhan Wu, Wenyu Dou, Xiaolin Yang, Tengfei Niu, Zhuzhen Han, Li Yang, Rufeng Wang, Zhengtao Wang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Exploring the Multifunctional Role ofInternational journal of molecular sciences · 2025
    Review
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

8 authors at 2 institutions in 1 country.

Zongzhan Wu *Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Wenyu Dou *Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Xiaolin YangInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Tengfei NiuInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Zhuzhen HanInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Li YangInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China.
Rufeng WangInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China. wrffrw0801@shutcm.edu.cn.ORCID http://orcid.org/0000-0001-5362-0420
Zhengtao WangInstitute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, People's Republic of China. ztwang@shutcm.edu.cn.
State Administration of Traditional Chinese Medicine of the People's Republic of China · CNShanghai University of Traditional Chinese Medicine · CN

Funding

National Natural Science Foundation of China 81603229National Natural Science Foundation of China 82373989Natural Science Foundation of Shanghai 20ZR1458200Shanghai Rising-Star Program 20QA1408800
6 · The paper itself

Abstract

Oleanane-type ginsenosides are a class of compounds with remarkable pharmacological activities. However, the lack of effective preparation methods for specific rare ginsenosides has hindered the exploration of their pharmacological properties. In this study, a novel glycoside hydrolase PlGH3 was cloned from Paenibacillus lactis 154 and heterologous expressed in Escherichia coli. Sequence analysis revealed that PlGH3 consists of 749 amino acids with a molecular weight of 89.5 kDa, exhibiting the characteristic features of the glycoside hydrolase 3 family. The enzymatic characterization results of PlGH3 showed that the optimal reaction pH and temperature was 8 and 50 °C by using p-nitrophenyl-β-D-glucopyranoside as a substrate, respectively. The K

Indexed as

GinsenosidesPaenibacillusSaponinsEscherichia coliEstersGlycoside HydrolasesMolecular Docking SimulationOleanolic AcidEstersGinsenosidesGlycoside HydrolasesoleananeOleanolic AcidSaponinsBiotransformationGlycoside hydrolase family 3Molecular dockingPseudoginsenoside RP1Tarasaponin VI

Identifiers

PMID38573330
PMCPMC10995091
OpenAlexW4393941355

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.