Evidence map›Paper›PMID 34874472›Full record

ArticleApplied microbiology and biotechnology2022

A highly versatile fungal glucosyltransferase for specific production of quercetin-7-O-β-D-glucoside and quercetin-3-O-β-D-glucoside in different hosts.

Jie Ren, Wenzhu Tang, Caleb Don Barton, Owen M Price, Mark Wayne Mortensen, Alexandra Phillips, Banner Wald, Simon Elgin Hulme, Logan Powell Stanley, Joan Hevel and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Therapeutic Potential ofPlants (Basel, Switzerland) · 2025
    Article
  3. Review
  4. 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

11 authors at 1 institution in 2 countries.

Jie RenDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Wenzhu TangDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Caleb Don BartonDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Owen M PriceDepartment of Chemistry and Biochemistry, Utah State University, 0300 Old Main Hill, Logan, UT, 84322-0300, USA.
Mark Wayne MortensenDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Alexandra PhillipsDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Banner WaldDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Simon Elgin HulmeDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Logan Powell StanleyDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
Joan HevelDepartment of Chemistry and Biochemistry, Utah State University, 0300 Old Main Hill, Logan, UT, 84322-0300, USA.ORCID http://orcid.org/0000-0002-9559-4635
Jixun ZhanDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA. jixun.zhan@usu.edu.ORCID http://orcid.org/0000-0003-0200-9183
Utah State University · US

Funding

Directorate for Engineering CBET-2044558
6 · The paper itself

Abstract

Glycosylation is an effective way to improve the water solubility of natural products. In this work, a novel glycosyltransferase gene (BbGT) was discovered from Beauveria bassiana ATCC 7159 and heterologously expressed in Escherichia coli. The purified enzyme was functionally characterized through in vitro enzymatic reactions as a UDP-glucosyltransferase, converting quercetin to five monoglucosylated and one diglucosylated products. The optimal pH and temperature for BbGT are 35 ℃ and 8.0, respectively. The activity of BbGT was stimulated by Ca

Indexed as

GlucosyltransferasesQuercetinEscherichia coliGlucosidesSaccharomyces cerevisiaeGlucosidesGlucosyltransferasesQuercetinBeauveria bassiana ATCC 7159GlucosyltransferaseHeterologous expressionQuercetin-3-O-β-D-glucosideQuercetin-7-O-β-D-glucoside

Identifiers

PMID34874472
OpenAlexW4200549758

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.