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Title: Investigation of bovine serum albumin denaturation using ultrasonic spectroscopy
Authors: Povey, Malcolm J.W.
Moore, Jonathan D.
Braybrook, Julian
Simons, Howard
Belchamber, Ron
Raganathan, Meera
Pinfield, Valerie J.
Keywords: Ultrasound spectroscopy
Bovine serum albumin
Protein-protein interactions
Protein-solvent interactions
Issue Date: 2011
Publisher: © Elsevier
Citation: POVEY, M.J.W., MOORE, J.D., BRAYBROOK, J. ... et al, 2011. Investigation of bovine serum albumin denaturation using ultrasonic spectroscopy. Food Hydrocolloids, 25 (5), pp.1233-1241.
Abstract: The ability of ultrasound spectroscopy to characterise protein denaturation at relatively high concentrations and under conditions found in foods, is examined. Measurement of longitudinal sound velocity against concentration and frequency (20-160 MHz) for the bovine serum albumin monomer at pH 7.0 gave a frequency independent value for molecular compressibility of at 25 °C, corresponding to a sound velocity for the BSA molecule of 1920 ms-1. At 160 MHz, the longitudinal sound attenuation in BSA molecules is ~5200 Npm-1, a factor of 10 higher than in water. The excess attenuation of the solution over water was nearly 90 Npm-1 at the highest measured volume fraction of 0.03 (or 3% v/v). Concentration-dependent ultrasound velocity (20 - 160 MHz) and attenuation (2 - 120 MHz) spectra were obtained over time for heated bovine serum albumin (BSA) solutions up to 40 mg/mL at neutral pH and at 25 °C. An acoustic scattering model was used which considered the solute molecules as scatterers of ultrasound, to determine the molecules' sound velocity, compressibility, and attenuation properties. Mild heat treatment caused the molecule to organise into dimers and trimers, without change in sound velocity; implying that there is little or no change in secondary structure. Changes in attenuation spectra correlated with estimated molecular weight as determined through DLS and SEC measurements. During oligomerisation, the BSA molecules continue to behave acoustically as monomers. Under severe heat treatment, BSA rapidly suffered irreversible denaturation and gelation occurred which affected both ultrasound attenuation spectra and the velocity of sound, consistent with significant molecular conformation changes and/or molecule-molecule interactions.
Description: This is the author’s version of a work that was accepted for publication in the journal Food Hydrocolloids. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published at: http://dx.doi.org/10.1016/j.foodhyd.2010.11.011
Version: Accepted for publication
DOI: 10.1016/j.foodhyd.2010.11.011
URI: https://dspace.lboro.ac.uk/2134/11088
Publisher Link: http://www.journals.elsevier.com/food-hydrocolloids/
ISSN: 0268-005X
Appears in Collections:Published Articles (Chemical Engineering)

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