title: Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli.
abstract: Hen egg white lysozyme was expressed as a protein fusion with the OmpA signal sequence and an octapeptide linker in Escherichia coli. The expression yielded soluble and enzymatically active lysozyme. Lysozyme activity was detected in the periplasmic space, in the cytosol and in the insoluble cytosolic fraction of E. coli. The results indicate that the environmental conditions in both the cytosol and the periplasmic space of E. coli were sufficient for correct protein folding and disulphide bond formation of eukaryotic recombinant lysozyme. However, the expression of active enzyme in E. coli consequently led to bacterial cell lysis due to hydrolysis of the peptidoglucan.
authors.affiliation: Department of Protein Engineering, AFRC Institute of Food Research, Reading, UK.
authors.forename: B
authors.initials: B
authors.lastname: Fischer
authors.forename: B
authors.initials: B
authors.lastname: Perry
authors.forename: G
authors.initials: G
authors.lastname: Phillips
authors.forename: I
authors.initials: I
authors.lastname: Sumner
authors.forename: P
authors.initials: P
authors.lastname: Goodenough
mesh_terms: D000818:Animals; D001709:Biotechnology; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005260:Female; D015870:Gene Expression; D009113:Muramidase / Q000096:biosynthesis* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D012995:Solubility
chemical_list: D011993:Recombinant Fusion Proteins; D009113:Muramidase