Biosynthetic characterization and biochemical features of the third natural nisin variant, nisin Q, produced by Lactococcus lactis 61-14
Article first published online: 19 NOV 2008
© 2008 The Authors. Journal compilation © 2008 The Society for Applied Microbiology
Journal of Applied Microbiology
Volume 105, Issue 6, pages 1982–1990, December 2008
How to Cite
Yoneyama, F., Fukao, M., Zendo, T., Nakayama, J. and Sonomoto, K. (2008), Biosynthetic characterization and biochemical features of the third natural nisin variant, nisin Q, produced by Lactococcus lactis 61-14. Journal of Applied Microbiology, 105: 1982–1990. doi: 10.1111/j.1365-2672.2008.03958.x
- Issue published online: 21 NOV 2008
- Article first published online: 19 NOV 2008
- 2007/1925: received 28 November 2007, revised 9 May 2008 and accepted: 4 June 2008
- lactic acid bacteria;
- Lactococcus lactis;
Aims: To characterize the genetic and biochemical features of nisin Q.
Methods and Results: The nisin Q gene cluster was sequenced, and 11 putative orfs having 82% homology with the nisin A biosynthesis gene cluster were identified. Nisin Q production was confirmed from the nisQ-introduced nisin Z producer. In the reporter assay, nisin Q exhibited an induction level that was threefold lower than that of nisin A. Nisin Q demonstrated an antimicrobial spectrum similar to those of the other nisins. Under oxidizing conditions, nisin Q retained a higher level of activity than nisin A. This higher oxidative tolerance could be attributed to the presence of only one methionine residue in nisin Q, in contrast to other nisins that contain two.
Conclusions: The 11 orfs of the nisin producers were identical with regard to their functions. The antimicrobial spectra of the three natural nisins were similar. Nisin Q demonstrated higher oxidative tolerance than nisin A.
Significance and Impact of the Study: Genetic and biochemical features of nisin Q are similar to those of other variants. Moreover, owing to its higher oxidative tolerance, nisin Q is a potential alternative for nisin A.