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Investigation of the structure of alpha-lactalbumin protein nanotubes using optical spectroscopy

Published online by Cambridge University Press:  19 December 2013

Özgür Tarhan ,
Enver Tarhan  and
Şebnem Harsa
Özgür Tarhan*
Affiliation:
Department of Food Engineering, Faculty of Engineering, Izmir Institute of Technology, Urla, Izmir TR-35430, Turkey
Enver Tarhan
Affiliation:
Department of Physics, Faculty of Science, Izmir Institute of Technology, Urla, Izmir TR-35430, Turkey
Şebnem Harsa
Affiliation:
Department of Food Engineering, Faculty of Engineering, Izmir Institute of Technology, Urla, Izmir TR-35430, Turkey
*
*For correspondence; e-mail: [email protected]
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Abstract

Alpha-lactalbumin (α-la) is one of the major proteins in whey. When partially hydrolysed with Bacillus licheniformis protease, it produces nanotubular structures in the presence of calcium ions by a self-assembly process. This study presents investigation of α-la protein structure during hydrolysis and nanotube formation using optical spectroscopy. Before spectroscopic measurements, nanotubes were examined with microscopy. The observed α-la nanotubes (α-LaNTs) were in the form of regular hollow strands with a diameter of about 20 nm and the average length of 1 μm. Amide and backbone vibration bands of the Raman spectra displayed remarkable conformational changes in α and β domains in the protein structure during nanotube growth. This was confirmed by the Fourier-transform infrared (FTIR) spectroscopy data. Also, FTIR analysis revealed certain bands at calcium (Ca++) binding sites of COO− groups in hydrolysed protein. These sites might be critical in nanotube elongation.

Keywords

α-Lactalbuminprotein nanotubesmicroscopyRamanFTIR
Type
Research Article
Information
Journal of Dairy Research , Volume 81 , Issue 1 , February 2014 , pp. 98 - 106
Copyright
Copyright © Proprietors of Journal of Dairy Research 2013 

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