Evidence map›Paper›PMID 40686639›Full record

ArticleRSC advances2025

Unravelling the influence of choline chloride-based deep eutectic solvents on lysozyme: a comparative study of fructose and formic acid donors.

Ntebogeng Mqoni, Sheldon Sookai, Ajit Kumar, Lebogang Katata-Seru, Faruq Mohammad, Pannuru Venkatesu, Indra Bahadur, Ahmed Abdullah Soleiman

Abstract read
In one paragraph

Article in RSC advances, 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

8 authors.

Ntebogeng MqoniDepartment of Chemistry, North-West University (Mafikeng Campus) Private Bag X2046 Mmabatho 2735 South Africa bahadur.indra@nwu.ac.za.ORCID https://orcid.org/0000-0001-5644-8937
Sheldon SookaiMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand PO WITS 2050 Johannesburg South Africa.ORCID https://orcid.org/0000-0003-3360-7338
Ajit KumarDiscipline of Microbiology, School of Life Sciences, College of Agriculture, Engineering and Science, University of KwaZulu-Natal (Westville Campus) Durban 4000 South Africa.
Lebogang Katata-SeruDepartment of Chemistry, North-West University (Mafikeng Campus) Private Bag X2046 Mmabatho 2735 South Africa bahadur.indra@nwu.ac.za.ORCID https://orcid.org/0000-0002-7228-305X
Faruq MohammadDepartment of Chemistry, College of Science, King Saud University P. O. Box 2455 Riyadh 11451 Kingdom of Saudi Arabia.ORCID https://orcid.org/0000-0002-9318-9986
Pannuru VenkatesuDepartment of Chemistry, University of Delhi Delhi 110 007 India pvenkatesu@chemistry.du.ac.in.ORCID https://orcid.org/0000-0002-8926-2861
Indra BahadurDepartment of Chemistry, North-West University (Mafikeng Campus) Private Bag X2046 Mmabatho 2735 South Africa bahadur.indra@nwu.ac.za.ORCID https://orcid.org/0000-0003-2906-473X
Ahmed Abdullah SoleimanDepartment of Chemistry, Southern University and A&M College Baton Rouge LA 70813 USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Advances in medicine and pharmaceutics have led to an increasing need for efficient structure stabilization methods for therapeutic proteins. Lysozyme is an antimicrobial enzyme present in mucosal secretions and animal and plant tissues and merited by a wide range of applications. However, its inherent vulnerability to high temperatures and external stress limits these applications. To overcome these drawbacks, biocompatible solvents (deep eutectic solvents (DESs)) are used to stabilize the structure and activity of lysozyme. Consequently, a comprehensive assessment was undertaken to evaluate the effects of two DES solutions-choline chloride-fructose (ChCl/F) and choline chloride-formic acid (ChCl/FA)-on the conformation, thermal stability and enzymatic activity of lysozyme. This was done using UV-visible spectroscopy, Fourier transform infrared (FTIR) spectroscopy, steady-state fluorescence, dynamic light scattering (DLS), circular dichroism (CD) measurements, transmission electron microscopy (TEM) and activity assays, as a function of DES concentration. ChCl/FA is shown to preserve the structural and thermal stability, and enhance the enzymatic activity of lysozyme, while ChCl/F was shown to destabilize lysozyme. Moreover, high concentrations of both DES solutions weaken the activity of lysozyme. Overall, DESs can be described as potential biocompatible, sustainable media for preservating the stability and activity of lysozyme.

Identifiers

PMID40686639
PMCPMC12272560

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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.