PHYSIOLOGICAL CONSEQUENCE OF EXPRESSION OF SOLUBLE AND ACTIVE HEN EGG-WHITE LYSOZYME IN ESCHERICHIA-COLI

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.