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Issue 50, 2020
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Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis

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Abstract

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 in vivo study using lysozyme to demonstrate the antigenic retention over long-term storage. The results suggest that protein is confined within the ensilicated material, and thus is unable to unfold and denature but is still functional after long-term storage.

Graphical abstract: Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis

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Supplementary files

Article information


Submitted
09 Jun 2020
Accepted
04 Aug 2020
First published
12 Aug 2020

This article is Open Access

RSC Adv., 2020,10, 29789-29796
Article type
Paper

Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis

A. Doekhie, M. N. Slade, L. Cliff, L. Weaver, R. Castaing, J. Paulin, Y.-C. Chen, K. J. Edler, F. Koumanov, K. J. Marchbank, J. M. H. van den Elsen and A. Sartbaeva, RSC Adv., 2020, 10, 29789
DOI: 10.1039/D0RA06412B

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    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
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    [Original citation] - Published by The Royal Society of Chemistry.

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