Evidence map›Paper›PMID 39275055›Full record

ArticleMolecules (Basel, Switzerland)2024

Thermal Stabilisation of Lysozyme through Ensilication.

Reveng A Abdulkareem, Aswin Doekhie, Nikoletta Fotaki, Francoise Koumanov, Charlotte A Dodson, Asel Sartbaeva

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Reveng A AbdulkareemDepartment of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Aswin DoekhieDepartment of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.ORCID 0000-0002-9612-7588
Nikoletta FotakiDepartment of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.ORCID 0000-0003-1826-7363
Francoise KoumanovDepartment for Health, Centre for Nutrition, Exercise and Metabolism, University of Bath, Claverton Down, Bath BA2 7AY, UK.ORCID 0000-0002-9029-3390
Charlotte A DodsonDepartment of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.ORCID 0000-0002-8403-726X
Asel SartbaevaDepartment of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.ORCID 0000-0003-1017-0161

Funding

Higher Committee for Education Development (HCED), Iraq Scholarship
6 · The paper itself

Abstract

Protein therapeutics, vaccines, and other commercial products are often sensitive to environmental factors, such as temperature and long-term storage. In many cases, long-term protein stability is achieved by refrigeration or freezing. One alternative is the encapsulation of the protein cargo within an inert silica matrix (ensilication) and storage or transport at room temperature as a dry powder. In this paper, we test the effect of three commonly used biological buffers on the ensilication, storage, and desilication of the enzyme lysozyme. We show that ensilication protects lysozyme from heat (100 °C for 1 h) and during storage (18 months at room temperature). The choice of ensilication buffer has little effect on the activity of lysozyme after desilication. Our results provide confidence in the continued pursuit of ensilication as a methodology for protein stabilisation and in its compatibility with biological buffers.

Indexed as

Enzyme StabilityMuramidaseSilicon DioxideBuffersHot TemperatureTemperatureBuffersMuramidaseSilicon Dioxideensilicationlysozymeprotein stabilisationsol–gel technology

Identifiers

PMID39275055
PMCPMC11396922

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.