Differential scanning calorimetry of native silk feedstock
Open accessAbstract
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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The exothermic event at ~233.0 °C in SF arises from ordering of previously amorphous or weakly organized chain segments into more stable β-sheet rich domains, a phenomenon commonly reported for semi-crystalline silk fibroin systems undergoing thermal treatment.
“This exothermic event arises from the ordering of previously amorphous or weakly organized chain segments into more stable β-sheet rich domains, a phenomenon commonly reported for semi-crystalline silk fibroin systems undergoing thermal treatment [45,46].”
From Montmorillonite-reinforced methacrylated collagen/methacrylated silk fibroin hydrogel-based inks: rheological and physicochemical characterization for bone scaffold applications (2026) · cites this paper as [45]
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Cited by
Sorted by citations
Antunes, B. S. L., Pedrini, F., Komatsu, D., Asami, J., Dicko, C., & Duek, E. A. R. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154129
- Authors
- Holland, C., Hawkins, N., Frydrych, M., Laity, P., Porter, D., & Vollrath, F.
- Affiliations
- University of Sheffield (GB)
- University of Oxford (GB)
- Corresponding author
- Holland, Chris
- Vollrath, Fritz
- Venue
- Macromolecular Bioscience
- Publisher
- Wiley
- Published
- 2018-11-09
- Volume
- 19
- Issue
- 3
- Pages
- e1800228-e1800228
- ISSN
- 1616-5187 (ISSN-L)
- 1616-5195
- OpenAlex
- W2899884703
- Cited by
- 18
- References
- 61
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 4 · 2019: 2
- FWCI
- 0.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Macromolecular Bioscience (publishedVersion, cc-by)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Funders
- Engineering and Physical Sciences Research Council (EP/K005693/1)
- H2020 Future and Emerging Technologies (713475)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Silkworms and Sericulture Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- thermal stability, protein denaturation, denaturation enthalpy, protein hydration, silk spinning
- MeSH terms
- Animals, Calorimetry, Differential Scanning, Hot Temperature, Bombyx, Silk
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