B. Fischer et al., PHYSIOLOGICAL CONSEQUENCE OF EXPRESSION OF SOLUBLE AND ACTIVE HEN EGG-WHITE LYSOZYME IN ESCHERICHIA-COLI, Applied microbiology and biotechnology, 39(4-5), 1993, pp. 537-540
Hen egg white lysozyme was expressed as a protein fusion with the OmpA
signal sequence and an octapeptide linker in Escherichia coli. The ex
pression yielded soluble and enzymatically active lysozyme. Lysozyme a
ctivity was detected in the periplasmic space, in the cytosol and in t
he insoluble cytosolic fraction of E. coli. The results indicate that
the environmental conditions in both the cytosol and the periplasmic s
pace of E. coli were sufficient for correct protein folding and disulp
hide bond formation of eukaryotic recombinant lysozyme. However, the e
xpression of active enzyme in E. coli consequently led to bacterial ce
ll lysis due to hydrolysis of the peptidoglucan.