Differential scanning calorimetry of native silk feedstock

Native silk proteins, extracted directly from the silk gland prior to spinning, offer access to a naturally hydrated protein that has undergone little to no processing. Combined with differential scanning calorimetry (DSC), it is possible to probe the thermal stability and hydration status of silk a...

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Hlavní autoři: Holland, C, Hawkins, N, Frydrych, M, Laity, P, Porter, D, Vollrath, F
Médium: Journal article
Jazyk:English
Vydáno: Wiley 2018
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author Holland, C
Hawkins, N
Frydrych, M
Laity, P
Porter, D
Vollrath, F
author_facet Holland, C
Hawkins, N
Frydrych, M
Laity, P
Porter, D
Vollrath, F
author_sort Holland, C
collection OXFORD
description Native silk proteins, extracted directly from the silk gland prior to spinning, offer access to a naturally hydrated protein that has undergone little to no processing. Combined with differential scanning calorimetry (DSC), it is possible to probe the thermal stability and hydration status of silk and thus investigate its denaturation and solidification, echoing that of the natural spinning process. It is found that native silk is stable between −10 °C and 55 °C, and both the high‐temperature enthalpy of denaturation (measured via modulated temperature DSC) and a newly reported low‐temperature ice‐melting transition may serve as useful quality indicators in the future for artificial silks. Finally, compared to albumin, silk's denaturation enthalpy is much lower than expected, which is interpreted within a recently proposed entropic desolvation framework which can serve to unveil the low‐energy aquamelt processing pathway.
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spelling oxford-uuid:86b44434-d9f3-41c6-a067-cbe644b6c9f52022-03-26T22:05:44ZDifferential scanning calorimetry of native silk feedstockJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:86b44434-d9f3-41c6-a067-cbe644b6c9f5EnglishSymplectic Elements at OxfordWiley2018Holland, CHawkins, NFrydrych, MLaity, PPorter, DVollrath, FNative silk proteins, extracted directly from the silk gland prior to spinning, offer access to a naturally hydrated protein that has undergone little to no processing. Combined with differential scanning calorimetry (DSC), it is possible to probe the thermal stability and hydration status of silk and thus investigate its denaturation and solidification, echoing that of the natural spinning process. It is found that native silk is stable between −10 °C and 55 °C, and both the high‐temperature enthalpy of denaturation (measured via modulated temperature DSC) and a newly reported low‐temperature ice‐melting transition may serve as useful quality indicators in the future for artificial silks. Finally, compared to albumin, silk's denaturation enthalpy is much lower than expected, which is interpreted within a recently proposed entropic desolvation framework which can serve to unveil the low‐energy aquamelt processing pathway.
spellingShingle Holland, C
Hawkins, N
Frydrych, M
Laity, P
Porter, D
Vollrath, F
Differential scanning calorimetry of native silk feedstock
title Differential scanning calorimetry of native silk feedstock
title_full Differential scanning calorimetry of native silk feedstock
title_fullStr Differential scanning calorimetry of native silk feedstock
title_full_unstemmed Differential scanning calorimetry of native silk feedstock
title_short Differential scanning calorimetry of native silk feedstock
title_sort differential scanning calorimetry of native silk feedstock
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