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Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis

Doekhie, A. ; Slade, M. N. ; Cliff, L. ; Weaver, L. ; Castaing, R. ; Paulin, J. ; Chen, Y.-C. ; Edler, K. J. LU orcid ; Koumanov, F. and Marchbank, K. J. , et al. (2020) In RSC Advances 10(50). p.29789-29796
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... (More)

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.

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publishing date
type
Contribution to journal
publication status
published
in
RSC Advances
volume
10
issue
50
pages
8 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:85090092993
ISSN
2046-2069
DOI
10.1039/d0ra06412b
language
English
LU publication?
no
additional info
Publisher Copyright: © The Royal Society of Chemistry.
id
80fe2296-8747-4906-ad80-d630d959bf4a
date added to LUP
2022-07-12 15:57:48
date last changed
2022-08-12 12:57:39
@article{80fe2296-8747-4906-ad80-d630d959bf4a,
  abstract     = {{<p>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.</p>}},
  author       = {{Doekhie, A. and Slade, M. N. and Cliff, L. and Weaver, L. and Castaing, R. and Paulin, J. and Chen, Y.-C. and Edler, K. J. and Koumanov, F. and Marchbank, K. J. and Van Den Elsen, J. M.H. and Sartbaeva, A.}},
  issn         = {{2046-2069}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{50}},
  pages        = {{29789--29796}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{RSC Advances}},
  title        = {{Thermal resilience of ensilicated lysozyme <i>via </i>calorimetric and <i>in</i> <i>vivo </i>analysis}},
  url          = {{http://dx.doi.org/10.1039/d0ra06412b}},
  doi          = {{10.1039/d0ra06412b}},
  volume       = {{10}},
  year         = {{2020}},
}