{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Doekhie A"],"funding":["Medical Research Council","University of Bath","Newcastle University","Biotechnology and Biological Sciences Research Council"],"pagination":["29789-29796"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9056174"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(50)"],"pubmed_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 sili"],"journal":["RSC advances"],"pubmed_title":["Thermal resilience of ensilicated lysozyme <i>via</i> calorimetric and <i>in vivo</i> analysis."],"pmcid":["PMC9056174"],"funding_grant_id":["BB/N022165/1","MC_PC_15030","MR/P002927/1","BH161151"],"pubmed_authors":["Slade MN","Doekhie A","Castaing R","Paulin J","Marchbank KJ","van den Elsen JMH","Chen YC","Cliff L","Sartbaeva A","Edler KJ","Weaver L","Koumanov F"],"additional_accession":[]},"is_claimable":false,"name":"Thermal resilience of ensilicated lysozyme <i>via</i> calorimetric and <i>in vivo</i> analysis.","description":"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 sili","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-05-31T05:05:38.543Z","creation":"2025-02-19T01:54:56.568Z"},"accession":"S-EPMC9056174","cross_references":{"pubmed":["35518265"],"doi":["10.1039/d0ra06412b"]}}