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Investigation of bovine serum albumin denaturation using ultrasonic spectroscopy.

Povey, M J W*; Moore, J D; Braybrook, J*; Simons, H*; Belchamber, R*; Raganathan, M*; Pinfield, V* (2011) Investigation of bovine serum albumin denaturation using ultrasonic spectroscopy. Food Hydrocolloids, 25 (5). pp. 1233-1241.

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Abstract

Concentration-dependent ultrasound velocity and attenuation spectra in the frequency range 2 -160 MHz for bovine serum albumin (BSA) solutions at neutral pH up to 40 mg/mL and at 25 °C, have been measured. Data is analysed by considering the solute molecules as scatterers of ultrasound, and applying a scattering model to determine the molecules' sound speed, compressibility, and attenuation properties in the solvated state. Less severe heat treatment caused the molecule to form dimers and trimers, no velocity changes were observed; with little or no molecular conformation change, changes in attenuation spectra were nevertheless manifest which correlated with DLS and SEC sizes. During oligomerisation, the BSA molecules continue to behave acoustically as individual particles.
BSA was then `cooked', irreversible denaturation and gelation of the protein affected both ultrasound attenuation spectra and the velocity of sound, consistent with significant molecular conformation changes. When significant denaturation occurs molecular compressibility changes significantly. The method demonstrates how important molecular properties can be obtained from ultrasound spectra for biomolecules in solution. The properties obtained are affected by the interactions of the biomolecule with the solvent.

Item Type: Article
Keywords: ultrasound spectroscopy, compressibility, conformational transitions, bovine serum albumin, BSA, gelation
Subjects: Biotechnology
Biotechnology > Biopharmaceutical Manufacturing and Characterisation
Identification number/DOI: 10.1016/j.foodhyd.2010.11.011
Last Modified: 02 Feb 2018 13:14
URI: http://eprintspublications.npl.co.uk/id/eprint/4945

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