Thesis-2000-Ayre.pdf (11.56 MB)
The adsorption of proteins onto ultrafiltration membranes
thesis
posted on 2018-10-09, 08:44 authored by Lorna M. AyreThe mass of five proteins (Bovine serum albumin (BSA), casein, lysozyme,
ovalbumin and pepsin) adsorbed to five different membrane materials (of various
hydrophobicities) was quantified using a static system and analysed to establish any
trends. Comparing the results from the five membranes it seems that there were no
obvious trends between the protein masses adsorbed indicating that it may not be just
one aspect of protein structure that is important in the adsorption process.
Many investigations have indicated that the protein may undergo a conformational
change during the adsorption process. Disulphide bridges contribute readily to the
stability of the protein molecule and it was hypothesised that if such a structural
change occurred, it would result in the breakage of these covalent bonds. To this end,
the free thiol group content of the proteins was quantified before and after adsorption. [Continues.]
History
School
- Aeronautical, Automotive, Chemical and Materials Engineering
Department
- Chemical Engineering
Publisher
© Lorna AyrePublisher statement
This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/Publication date
2000Notes
A Doctoral Thesis. Submitted in partial fulfilment of the requirements for the award of Doctor of Philosophy at Loughborough University.Language
- en