Holland, C. orcid.org/0000-0003-0913-2221, Hawkins, N., Frydrych, M. orcid.org/0000-0003-0022-6934 et al. (3 more authors) (2019) Differential scanning calorimetry of native silk feedstock. Macromolecular Bioscience, 19 (3). 1800228. ISSN 1616-5187
Abstract
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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2018 The Authors. Published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
Keywords: | Bombyx mori; denaturation; differential scanning calorimetry; protein; silk |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Engineering (Sheffield) > Department of Materials Science and Engineering (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 31 Jan 2019 10:38 |
Last Modified: | 27 Oct 2021 10:18 |
Status: | Published |
Publisher: | Wiley |
Refereed: | Yes |
Identification Number: | 10.1002/mabi.201800228 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:138861 |
Download
Filename: Holland_et_al-2018-Macromolecular_Bioscience.pdf
Licence: CC-BY 4.0