Structure and Biological Activity of Chemically Modified Nisin A Species
Article first published online: 23 JUL 2004
European Journal of Biochemistry
Volume 241, Issue 3, pages 716–722, November 1996
How to Cite
Rollema, H. S., Metzger, J. W., Both, P., Kuipers, O. P. and Siezen, R. J. (1996), Structure and Biological Activity of Chemically Modified Nisin A Species. European Journal of Biochemistry, 241: 716–722. doi: 10.1111/j.1432-1033.1996.00716.x
- Issue published online: 23 JUL 2004
- Article first published online: 23 JUL 2004
- (Received 21 May/12 August 1996) – EJB 96 0742/3
- chemically modified nisin;
- mass spectrometry;
Nisin, a 34-residue peptide bacteriocin, contains the less common amino acids lanthionine, β-methyl-lanthionine, dehydroalanine (Dha), and dehydrobutyrine (Dhb). Several chemically modified nisin A species were purified by reverse-phase HPLC and characterized by two-dimensional NMR and electrospray mass spectrometry. Five constituents, [2-hydroxy-Ala5]nisin, [Ile4-amide,pyruvyl-Leu6]des-Dha5-nisin, [Met(O)21]nisin, [Ser33]nisin, and nisin-(1–32)-peptide amide, were found in a commercial nisin sample. A further species, [2-hydroxy-Ala5]nisin-(1–32)-peptide amide, was obtained by freeze drying an acidic nisin solution. These compounds are formed by chemical modification of nisin: the addition of a water molecule to the dehydroalanine residues, which can lead to the cleavage of the polypeptide chain, or the oxidation of methionine residues.
The 2-hydroxyalanine-containing products have a limited stability; they are spontaneously converted into the corresponding des-dehydroalanine derivatives. The growth-inhibiting activity of the modified nisins towards different bacteria was determined. The 2-hydroxyalanine-containing species and the des-dehydroalanine derivative show a strong reduction in biological activity as compared to native nisin. [Met(O)21]nisin and [Ser33]nisin show moderate or no reduction in biological activity.