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nisin : ウィキペディア英語版
nisin

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Nisin is a polycyclic antibacterial peptide produced by the bacterium ''Lactococcus lactis'' used as a food preservative. It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha) and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine residues to the didehydro amino acids result in the multiple (5) thioether bridges.
Subtilin and epidermin are related to nisin. All are members of a class of molecules known as lantibiotics.
In the food industry, nisin is obtained from the culturing of ''L. lactis'' on natural substrates, such as milk or dextrose, and is not chemically synthesized.
It was originally isolated in the late 1930s, and produced since the 1950s as Nisaplin from naturally occurring sources by Aplin and Barrett in laboratories in Beaminster in Dorset,and approved as an additive for food use in the USA in the late 1960s, though the Beaminster factory is now owned by DuPont.
==Properties==
While in general most bacteriocins inhibit only closely related species, nisin is a rare example of a "broad-spectrum" bacteriocin effective against many Gram-positive organisms, including lactic acid bacteria (commonly associated with spoilage),'' Listeria monocytogenes'' (a known pathogen), ''Staphylococcus aureus'', ''Bacillus cereus'', ''Clostridium botulinum'', etc. It is also particularly effective against spores. Gram-negative bacteria are protected by their outer membrane but may become susceptible to nisin action after a heat shock or when this is coupled with the chelator EDTA. Nisin is soluble in water and can be effective at levels nearing the parts-per-billion range.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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