Chromatographic Analysis of Recombinant Lysostaphin Expressed in Escherichia coli

Jennings, Claire (2011) Chromatographic Analysis of Recombinant Lysostaphin Expressed in Escherichia coli. Doctoral thesis, Northumbria University.

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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.

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