Thiophilic chromatographic separations for large scale purification of whey proteins

Hdl Handle:
http://hdl.handle.net/10149/98820
Title:
Thiophilic chromatographic separations for large scale purification of whey proteins
Book Title:
Separations for biotechnology 3
Authors:
Noel, R. J. (Richard); Street, G. (Graham); O'Hare, W. T. (Liam)
Editors:
Pyle, D. L.
Affiliation:
University of Teesside. Chemical and Biochemical Engineering Research Centre.
Citation:
Noel, R. J., Street, G. and O'Hare, W. T. (1994) 'Thiophilic chromatographic separations for large scale purification of whey proteins' Third international symposium of the society of chemical industry, Reading, England, September 12 - 15, in Pyle, D. L. (ed) Separations for biotechnology 3. Cambridge: The Royal Society of Chemistry, pp.372-377.
Publisher:
Royal Society of Chemistry 3
Conference:
Third international symposium of the society of chemical industry, Reading, England, September 12 - 15, 1994
Issue Date:
1994
URI:
http://hdl.handle.net/10149/98820
Abstract:
A solid-phase material suitable for large-scale chromatography should possess a high binding capacity for the target protein and have a high specificity of binding, in order to produce high purity products in a single step operation. The matrix and the attached ligand should be stable to cleaning solutions such as 0.5M sodium hydroxide. The ligand should be non-toxic and show and low rate of leakage from the matrix. Finally the ligand should be inexpensive to produce and immobilise onto the solid-phase matrix. Thiophilic chromatography has been used to purify immunoglobulins from bovine and human colostral whey (1,2) and may have the potential to be suitable for large scale operation. The first thiophilic chromatography matrix (T-gel) was produced by reacting divinylsulphone-activated agarose wth 2-mercaptoethanol. It has the chemical structure, P-OCH2CH2SO2CH2CH2SCH2CH2Oh where P represents the solid-phase. This small non-toxic ligand was shown to purify immunoglobulins from blood serum (3,4,5), tissue culture supernatants (6) and ascites fluid (7,8) in the presence of ammonium and potassium sulphate salts. High purity (>90%) separations of immunoglobulins can be acheived in a single step. Modifications to the chemical structure of the ligand have been made (7) in an attempt to improve the purity of immunoglobulins produced from a tissue culture supernatant. The aims of this study are to determine the optimal conditions for the purification of immunoglobulins from cheese whey uing T-gel and to evaluate the separations performed by modified T-gel ligands. The suitability of thiophilic ligands for process scale purifictions from cheese whey are discussed in view of the results obtained.
Type:
Meetings and Proceedings; Book Chapter
Language:
en
Keywords:
immunoglobulin; chromatography; thiophilic; whey; purification
ISBN:
9780851867243
Citation Count:
0 [Web of Science, 14/05/2010]

Full metadata record

DC FieldValue Language
dc.contributor.authorNoel, R. J. (Richard)en
dc.contributor.authorStreet, G. (Graham)en
dc.contributor.authorO'Hare, W. T. (Liam)en
dc.contributor.editorPyle, D. L.en
dc.date.accessioned2010-05-14T10:58:49Z-
dc.date.available2010-05-14T10:58:49Z-
dc.date.issued1994-
dc.identifier.isbn9780851867243-
dc.identifier.urihttp://hdl.handle.net/10149/98820-
dc.description.abstractA solid-phase material suitable for large-scale chromatography should possess a high binding capacity for the target protein and have a high specificity of binding, in order to produce high purity products in a single step operation. The matrix and the attached ligand should be stable to cleaning solutions such as 0.5M sodium hydroxide. The ligand should be non-toxic and show and low rate of leakage from the matrix. Finally the ligand should be inexpensive to produce and immobilise onto the solid-phase matrix. Thiophilic chromatography has been used to purify immunoglobulins from bovine and human colostral whey (1,2) and may have the potential to be suitable for large scale operation. The first thiophilic chromatography matrix (T-gel) was produced by reacting divinylsulphone-activated agarose wth 2-mercaptoethanol. It has the chemical structure, P-OCH2CH2SO2CH2CH2SCH2CH2Oh where P represents the solid-phase. This small non-toxic ligand was shown to purify immunoglobulins from blood serum (3,4,5), tissue culture supernatants (6) and ascites fluid (7,8) in the presence of ammonium and potassium sulphate salts. High purity (>90%) separations of immunoglobulins can be acheived in a single step. Modifications to the chemical structure of the ligand have been made (7) in an attempt to improve the purity of immunoglobulins produced from a tissue culture supernatant. The aims of this study are to determine the optimal conditions for the purification of immunoglobulins from cheese whey uing T-gel and to evaluate the separations performed by modified T-gel ligands. The suitability of thiophilic ligands for process scale purifictions from cheese whey are discussed in view of the results obtained.en
dc.language.isoenen
dc.publisherRoyal Society of Chemistry 3en
dc.subjectimmunoglobulin-
dc.subjectchromatography-
dc.subjectthiophilic-
dc.subjectwhey-
dc.subjectpurification-
dc.titleThiophilic chromatographic separations for large scale purification of whey proteinsen
dc.typeMeetings and Proceedingsen
dc.typeBook Chapteren
dc.contributor.departmentUniversity of Teesside. Chemical and Biochemical Engineering Research Centre.en
dc.title.bookSeparations for biotechnology 3en
dc.identifier.conferenceThird international symposium of the society of chemical industry, Reading, England, September 12 - 15, 1994en
ref.citationcount0 [Web of Science, 14/05/2010]en
or.citation.harvardNoel, R. J., Street, G. and O'Hare, W. T. (1994) 'Thiophilic chromatographic separations for large scale purification of whey proteins' Third international symposium of the society of chemical industry, Reading, England, September 12 - 15, in Pyle, D. L. (ed) Separations for biotechnology 3. Cambridge: The Royal Society of Chemistry, pp.372-377.-
prism.startingPage372-
prism.endingPage377-
All Items in TeesRep are protected by copyright, with all rights reserved, unless otherwise indicated.