Nisin is a bacteriocin produced by Lactococcus lactis subsp. lactis, which is active against Gram-positive organisms including bacterial spores. It is not generally active against Gram-negative bacteria, yeasts and fungi. Gram negatives show nisin-sensitivity when their outer membrane permeability is altered by various means, such as treatments with chelators, e.g. EDTA, osmotic shock, heating, freezing, freeze-drying, high- pressure etc. Application of chelators and nisin is effective against Gram-negatives when exogenous nisin is added. Nisin produced in situ and chelators are not an effective combination, since nisin production follows the pH drop caused by sugar fermentation, and this interferes with the sequestering ability of the chelators. Presence of nisin during thermal inactivation of Gram-negatives though is effective. Bacteria become structurally injured during heating showing sensitivity to agents like SDS and deoxycholate and extended detection times by impedimetry. These injured bacteria are inactivated by nisin, with a concomitant reduction of the measured D-values. Low pH and the presence of small amount of chelators enhance the injury and inactivation and reduce D-values further. Gram-negative bacteria injured by chilling and freezing are also sensitive to nisin. The effectiveness of nisin is reduced in a food environment mostly of nisin binding to fat, and food particles. D-values were decreased less or not at all in egg white and liquid whole egg, respectively, and rapid chilling of bacteria attached to chicken skin in presence of nisin did not give the effect seen in laboratory media. Nisin is active against heat-, chill-, and freezing-stressed Gram-negatives only if it is present during the treatments. When the stress factor is removed, the bacteria recover their nisin resistance, implying transient susceptibility to nisin, but not to smaller molecules. This is probably due to rapid reorganisation and restoration of OM permeability damage, rather than biochemical repair. The LPS chain length influences the sensitisation of Gram-negatives to nisin, only in the case of freezing, where the strain with the shorter LPS chain was more sensitive than the wild type. Heat-, and freezing-stressed bacteria lost lipopolysaccharides and increased their cell surface hydrophobicity. This was not seen with chill-stressed bacteria, which were sensitive to nisin though. This indicates that release of LPS is not a prerequisite for nisin sensitivity in Gram-negatives.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:301293 |
| Date | January 2000 |
| Creators | Boziaris, Ioannis S. |
| Publisher | University of Surrey |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://epubs.surrey.ac.uk/842954/ |
Page generated in 0.002 seconds