Lysozyme expression in Lactococcus lactis.
Three lysozyme-encoding genes, one of eukaryotic and two of prokaryotic origin, were expressed in Lactococcus lactis subsp. lactis. Hen egg white lysozyme (HEL) could be detected in L. lactis lysates by Western blotting. No lysozyme activity was observed, however, presumably because of the absence of correctly formed disulphide bonds in the L. lactis product. The functionally related lysozymes of the E. coli bacteriophages T4 and lambda were produced as biologically active proteins in L. lactis. In both cases, the highest expression levels were obtained using configurations in which the bacteriophage lysozyme genes had been translationally coupled to a short open reading frame of lactococcal origin. Both enzymes, like HEL, may prevent the growth of food-spoilage bacteria.
Department of Genetics, University of Groningen, Haren, The Netherlands.
M
M
van de Guchte
F J
FJ
van der Wal
J
J
Kok
G
G
Venema
D010582:Bacteriophage lambda / Q000201:enzymology*; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D004529:Egg White; D015870:Gene Expression; D013294:Lactococcus lactis / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000096:biosynthesis / Q000235:genetics*; D010957:Plasmids / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D013604:T-Phages / Q000201:enzymology*
D011993:Recombinant Fusion Proteins; D009113:Muramidase