Affiliation:
1. Department of Food Science, Agricultural University of Wageningen, 6703 HD Wageningen, The Netherlands
2. Department of Microbiology, Netherlands Institute for Dairy Research, 6710 BA Ede, The Netherlands
3. Laboratoire des Biomembranes, Centre National de la Recherche Scientifique, Université Paris Sud, 91405 Orsay Cedex, France
Abstract
Nisin Z, a natural nisin variant, was recently isolated from
Lactococcus lactis
subspecies
lactis
NIZO 22186. The gene for this lantibiotic, designated
nisZ
, has been cloned, and its nucleotide sequence was found to be identical to that of the precursor nisin gene with the exception of a single mutation resulting in the substitution of Asn-27 for His-27 in the mature polypeptide (J. W. M. Mulders, I. J. Boerrigter, H. S. Rollema, R. J. Siezen, and W. M. de Vos, Eur. J. Biochem. 201:581-584, 1991). A K
+
electrode was used to investigate the effect of various environmental parameters on the action of nisin Z against
Listeria monocytogenes
. Addition of nisin Z resulted in immediate loss of cell K
+
, depolarization of the cytoplasmic membrane, inhibition of respiratory activity, and hydrolysis and partial efflux of cellular ATP. The action of nisin Z was optimal at pH 6.0 and was significantly reduced by di- and trivalent cations. The lanthanide gadolinium (Gd
3+
) was an efficient inhibitor and prevented nisin Z activity completely at a concentration of 0.2 mM. Nisin Z-induced loss of cell K
+
was reduced at low temperatures, presumably as a result of the increased ordering of the lipid hydrocarbon chains in the cytoplasmic membrane. In cells grown at 30°C, the action of nisin Z was prevented below 7°C, whereas in cells grown at 4°C nisin Z was able to induce K
+
leakage at this low temperature.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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