Thermal resilience of ensilicated lysozyme
Journal
RSC advances
ISSN: 2046-2069
Titre abrégé: RSC Adv
Pays: England
ID NLM: 101581657
Informations de publication
Date de publication:
10 Aug 2020
10 Aug 2020
Historique:
received:
09
06
2020
accepted:
04
08
2020
entrez:
6
5
2022
pubmed:
12
8
2020
medline:
12
8
2020
Statut:
epublish
Résumé
Ensilication is a novel method of protein thermal stabilisation using silica. It uses a modified sol-gel process which tailor fits a protective silica shell around the solvent accessible protein surface. This, electrostatically attached, shell has been found to protect the protein against thermal influences and retains its native structure and function after release. Here, we report the calorimetric analysis of an ensilicated model protein, hen egg-white lysozyme (HEWL) under several ensilication conditions. DSC, TGA-DTA-MS, CD, were used to determine unfolding temperatures of native, released and ensilicated lysozyme to verify the thermal resilience of the ensilicated material. Our findings indicate that ensilication protects against thermal fluctuations even at low concentrations of silica used for ensilication. Secondly, the thermal stabilisation is comparable to lyophilisation, and in some cases is even greater than lyophilisation. Additionally, we performed a mouse
Identifiants
pubmed: 35518265
doi: 10.1039/d0ra06412b
pii: d0ra06412b
pmc: PMC9056174
doi:
Types de publication
Journal Article
Langues
eng
Pagination
29789-29796Subventions
Organisme : Medical Research Council
ID : MC_PC_15030
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/P002927/1
Pays : United Kingdom
Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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