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Thermally resolved synchrotron FT-IR microscopy of structural changes in bloodmeal-based thermoplastics

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Abstract

Synchrotron FT-IR micro-spectroscopy was used to determine thermally induced structural changes in thermoplastic protein produced from bloodmeal after mixing with sodium sulphite, sodium dodecyl sulphate, urea, tri-ethylene glycol and water. Changes in protein secondary structure at elevated temperature were assessed using second derivative peak height ratios in the amide III region (1,200–1,330 cm−1) and compared with DSC and DMA results over the same temperature range. The results show an increase in ordered β-sheet structures with temperature at the expense of random coils, and that these β-sheets do not melt in the temperature range up to extrusion temperature of 120 °C. The implication of this is that during melt processing, β-sheet clusters may remain intact, similar to dispersed particulate fillers.

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Acknowledgements

This research was undertaken on the infrared microspectroscopy beamline at the Australian Synchrotron, Clayton, VIC, Australia. Proposal number AS122/IRMFI/4951. The authors would especially like to acknowledge the technical assistance of Dr. Mark Tobin and Dr. Danielle Martin. Travel funding support was received from the New Zealand Synchrotron Group Ltd.

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  1. School of Engineering, University of Waikato, Private Bag 3105, Hamilton, 3240, New Zealand

    James Michael Bier, Casparus Johannes Reinhard Verbeek & Mark Christopher Lay

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  1. James Michael Bier
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  2. Casparus Johannes Reinhard Verbeek
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  3. Mark Christopher Lay
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Correspondence to James Michael Bier.

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Bier, J.M., Verbeek, C.J.R. & Lay, M.C. Thermally resolved synchrotron FT-IR microscopy of structural changes in bloodmeal-based thermoplastics. J Therm Anal Calorim 115, 433–441 (2014). https://doi.org/10.1007/s10973-013-3340-8

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  • DOI: https://doi.org/10.1007/s10973-013-3340-8

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