Evidence map›Paper›PMID 40563441›Full record

ArticleBiomolecules2025

β-Galactosidase-Catalyzed Transglycosylation of Tyrosol: Substrates and Deep Eutectic Solvents Affecting Activity and Stability.

Alžbeta Koššuthová, Monika Antošová, Vladena Bauerová-Hlinková, Jacob A Bauer, Milan Polakovič

Abstract read
In one paragraph

Article in Biomolecules, 2025. 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
–field-weighted citation impact
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. 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

5 authors.

Alžbeta KoššuthováDepartment of Chemical and Biochemical Engineering, Institute of Chemical and Environmental Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37 Bratislava, Slovakia.
Monika AntošováDepartment of Chemical and Biochemical Engineering, Institute of Chemical and Environmental Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37 Bratislava, Slovakia.ORCID 0000-0003-3671-9108
Vladena Bauerová-HlinkováDepartment of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, 845 51 Bratislava, Slovakia.ORCID 0000-0003-0777-4407
Jacob A BauerDepartment of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, 845 51 Bratislava, Slovakia.ORCID 0000-0002-1396-1340
Milan PolakovičDepartment of Chemical and Biochemical Engineering, Institute of Chemical and Environmental Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37 Bratislava, Slovakia.ORCID 0000-0003-0238-8996

Funding

Slovak Research and Development Agency APVV-20-0312Slovak Research and Development Agency APVV-23-0448the Scientific Grant Agency of the Ministry of Education, Research, Development and Youth of the Slovak Republic and the Slovak Academy of Sciences VEGA 1/0515/22the Scientific Grant Agency of the Ministry of Education, Research, Development and Youth of the Slovak Republic and the Slovak Academy of Sciences VEGA 2/0081/24
6 · The paper itself

Abstract

β-Galactosidase, a glycoside hydrolase enzyme, also possesses glycosyl transferase activity and can glycosylate various aglycones, including tyrosol, a phenylethanoid with antioxidant and health-promoting effects. This study examines the effect of lactose, tyrosol and deep eutectic solvents (DESs) as co-solvents on the stability and activity of

Indexed as

beta-GalactosidaseDeep Eutectic SolventsPhenylethyl AlcoholAspergillus oryzaeBiocatalysisEnzyme StabilityGalactosidesGlycosylationLactoseSubstrate Specificity4-hydroxyphenylethanolbeta-GalactosidaseDeep Eutectic SolventsGalactosidesLactosePhenylethyl Alcoholdeep eutectic solventsenzyme activityphenylethanoidthermal stabilitytransglycosylationβ-galactosidase

Identifiers

PMID40563441
PMCPMC12191228

What OpenQuestion holds

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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.