• English
    • Welsh
  • English 
    • English
    • Welsh
  • Login
Search DSpace:
  • Home
  • Research at Cardiff Met
  • Library Services
  • Contact Us
View item 
  • DSpace home
  • Cardiff School of Sport and Health Sciences
  • Research Degrees (Sport and Health Sciences)
  • Research Degrees (Health Sciences)
  • View item
  • DSpace home
  • Cardiff School of Sport and Health Sciences
  • Research Degrees (Sport and Health Sciences)
  • Research Degrees (Health Sciences)
  • View item
JavaScript is disabled for your browser. Some features of this site may not work without it.

The development of new and improved methods for downstream purification of proteins and enzymes from crude mixtures

Thumbnail
View/open
Thesis (9.424Mb)
Author
Isgrove, Frances Helen
Date
2000
Type
Thesis
Publisher
Cardiff Metropolitan University
Metadata
Show full item record
Abstract
New economically viable methods for the industrial scale production and processing of proteins are constantly being sought. This project concentrates on two techniques which may be utilised in the purification of non-recombinant proteins. First, aqueous two-phase systems were investigated as a potential tool for the separation of individual proteose peptones from a total proteose peptone fraction of bovine milk. The optimum pH for the separation of β-CN-5P from the total proteose peptone components was pH7. Aqueous two-phase systems containing PEG with a mean molecular weight of less than 8000 were not found to separate the total proteose peptone components. The addition of sodium chloride into the aqueous two-phase systems encouraged a more effective extraction of β-CN-5P, although this effect was found to plateau at 5% NaCl. Second, a model enzyme was immobilised onto nylon film and the optimisation of binding conditions was studied using spectrophotometric procedures. Results suggested that slight variations in the concentration of the incubating solutions had a profound effect on the efficacy of the procedure. Additionally, a considerable quantity of observed binding appeared to be due to non-specific interactions between the ligand and the matrix. This binding was investigated and was found to be a result of both ionic and hydrophobic interactions.
URI
http://hdl.handle.net/10369/5578
Description
PhD
Collections
  • Research Degrees (Health Sciences) [111]

Browse

DSpace at Cardiff MetCommunities & CollectionsBy issue dateAuthorsTitlesSubjectsThis collectionBy issue dateAuthorsTitlesSubjects

My Account

Login

Statistics

Most Popular ItemsStatistics by CountryMost Popular Authors

DSpace software copyright © 2002-2015  DuraSpace
Contact us | Send feedback | Administrator