Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.588273
Title: Chromatographic analysis of recombinant lysostaphin expressed in Escherichia coli
Author: Jennings, Claire
Awarding Body: Northumbria University
Current Institution: Northumbria University
Date of Award: 2011
Availability of Full Text:
Access from EThOS:
Full text unavailable from EThOS. Please try the link below.
Access from Institution:
Abstract:
Lysostaphin (EC.3.4.24.75) is an extracellular glycylglycine endopeptidase produced exclusively by Staphylococcus simulans biovar staphylolyticus (ATCC 1362, NRRL B-2628). The zinc-containing endopeptidase demonstrates specific and potent staphylolytic activity therefore shows great promise for the treatment of blood-borne and biofilm-associated staphylococcal infections. The gene encoding mature lysostaphin has therefore been cloned and expressed using Escherichia coli, the most widely used expression host for recombinant protein production. Lysostaphin (EC.3.4.24.75) is an extracellular glycylglycine endopeptidase produced exclusively by Staphylococcus simulans biovar staphylolyticus (ATCC 1362, NRRL B-2628). The zinc-containing endopeptidase demonstrates specific and potent staphylolytic activity therefore shows great promise for the treatment of blood-borne and biofilm-associated staphylococcal infections. The gene encoding mature lysostaphin has therefore been cloned and expressed using Escherichia coli, the most widely used expression host for recombinant protein production. Lysostaphin (EC.3.4.24.75) is an extracellular glycylglycine endopeptidase produced exclusively by Staphylococcus simulans biovar staphylolyticus (ATCC 1362, NRRL B-2628). The zinc-containing endopeptidase demonstrates specific and potent staphylolytic activity therefore shows great promise for the treatment of blood-borne and biofilm-associated staphylococcal infections. The gene encoding mature lysostaphin has therefore been cloned and expressed using Escherichia coli, the most widely used expression host for recombinant protein production. Overall these findings are of concern for the production of recombinant protein production using E. coli. However this research suggested that chromatography can be used to sensitively detect and monitor product heterogeneity, so that a more homogeneous product could be produced by careful adjustment of expression, harvest and formulation conditions.
Supervisor: Black, Gary Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.588273  DOI: Not available
Keywords: F100 Chemistry
Share: