Evidence map›Paper›PMID 37782456›Full record

ArticleApplied biochemistry and biotechnology2024

Engineered β-glycosidase from Hyperthermophilic Sulfolobus solfataricus with Improved Rd-hydrolyzing Activity for Ginsenoside Compound K Production.

Chenchen Fu, Wenfeng Shen, Weina Li, Pan Wang, Luo Liu, Yangfang Dong, Jing He, Daidi Fan

Abstract read
PubMed Publisher
In one paragraph

Article in Applied biochemistry 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
0.3field-weighted citation impact, top 36% 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, 2 citations in OpenAlex.

  1. 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.

Chenchen FuShaanxi Key Laboratory of Degradable Biomedical Materials, Shaanxi R&D Center of Biomaterials and Fermentation Engineering, Biotech. & Biomed. Research Institute, School of Chemical Engineering, Northwest University, Shaanxi, 710069, China.
Wenfeng ShenShaanxi Key Laboratory of Degradable Biomedical Materials, Shaanxi R&D Center of Biomaterials and Fermentation Engineering, Biotech. & Biomed. Research Institute, School of Chemical Engineering, Northwest University, Shaanxi, 710069, China.
Weina LiShaanxi Key Laboratory of Degradable Biomedical Materials, Shaanxi R&D Center of Biomaterials and Fermentation Engineering, Biotech. & Biomed. Research Institute, School of Chemical Engineering, Northwest University, Shaanxi, 710069, China. 20154798@nwu.edu.cn.ORCID http://orcid.org/0000-0003-3198-1115
Pan WangShaanxi Key Laboratory of Degradable Biomedical Materials, Shaanxi R&D Center of Biomaterials and Fermentation Engineering, Biotech. & Biomed. Research Institute, School of Chemical Engineering, Northwest University, Shaanxi, 710069, China.
Luo LiuBeijing Bioprocess Key Laboratory, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
Yangfang DongShaanxi Giant Biogene Co., Ltd, Xi'an, 710065, Shaanxi, China.
Jing HeXi'an Giant Biogene Co., Ltd, Xi'an, 710065, Shaanxi, China.
Daidi FanShaanxi Key Laboratory of Degradable Biomedical Materials, Shaanxi R&D Center of Biomaterials and Fermentation Engineering, Biotech. & Biomed. Research Institute, School of Chemical Engineering, Northwest University, Shaanxi, 710069, China. fandaidi@nwu.edu.cn.
Northwest University · CNBeijing University of Chemical Technology · CN

Funding

National Natural Science Foundation of China 21706211National Natural Science Foundation of China 22108229the National Key R&D Program of China 2021YFC2101000the National Key R&D Program of China 2021YFC2101500, 2019YFA0905200
6 · The paper itself

Abstract

Hyperthermophilic Sulfolobus solfataricus β-glycosidase (SS-βGly), with higher stability and activity than mesophilic enzymes, has potential for industrial ginsenosides biotransformation. However, its relatively low ginsenoside Rd-hydrolyzing activity limits the production of pharmaceutically active minor ginsenoside compound K (CK). In this study, first, we used molecular docking to predict the key enzyme residues that may hypothetically interact with ginsenoside Rd. Then, based on sequence alignment and alanine scanning mutagenesis approach, key variant sites were identified that might improve the enzyme catalytic efficiency. The enzyme catalytic efficiency (k

Indexed as

GinsenosidesSulfolobus solfataricusArchaeal Proteinsbeta-GlucosidaseGlucosidasesGlycoside HydrolasesHydrolysisKineticsMolecular Docking SimulationMolecular Dynamics SimulationProtein EngineeringArchaeal Proteinsbeta-Glucosidaseginsenoside compound Kginsenoside RdGinsenosidesGlucosidasesGlycoside HydrolasesSulfolobus solfataricus beta-glycosidaseAlanine scanning mutagenesisGinsenoside Rd hydrolysisGinsenosides biotransformationGinsenosides compound KGlycosidase enzyme designing

Identifiers

PMID37782456
OpenAlexW4387241520

What OpenQuestion holds

Textmetadata
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.