We know that, Nisin is a polycyclic antibacterial peptide with 34 amino acid residues used as a food preservative. It contains 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.
Nisin is produced by fermentation using the bacterium Lactococcus lactis. Commercially, it is obtained from the culturing ofLactoccus lactis on natural substrates, such as milk or dextrose, and is not chemically synthesized.
The study is the first to show CHAC1's new role in promoting cancer cell death under nisin treatment. The findings also suggest that nisin may work by creating pores in the cancer cell membranes that allow an influx of calcium. It's unclear what role calcium plays in nisin-triggered cell death, but it's well known that calcium is a key regulator in cell death and survival.
Ref : http://onlinelibrary.wiley.com/doi/10.1002/cam4.35/abstract;jsessionid=288DD01F2898095E16F5EEAFEF5274FD.d02t03
Common food preservative may slow, even stop tumor growth
