International Journal of Current Research and Review
ISSN: 2231-2196 (Print)ISSN: 0975-5241 (Online)
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IJCRR - Vol 07 Issue 02, January, 2015

Pages: 47-53

Date of Publication: 30-Nov--0001

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Author: Sukrita Punyauppa-path, Parichat Phumkhachorn, Pongsak Rattanachaikunsopon

Category: Healthcare

Abstract:Nisin is a heat stable lantibiotic consisting of 34 amino acids. Of these amino acids, there are several unusual amino acids including dehydroalanine, dehydrobutyrine, aminobutyric acid, lanthionine and \?-methyllanthionine. It has antimicrobial activity against many species of Gram positive bacteria, but not Gram negative bacteria due to their outer membrane barriers. However, when used in combination with other chemical or physical treatments that destabilize the outer membranes, nisin can inhibit Gram negative bacteria. Nisin has been used as a food preservative in many food industries because it is legally approved as safe for use in food and beverage. The knowledge on the production and mechanism of antimicrobial action of nisin is important for the understanding how nisin contains unusual amino acids and how it kills sensitive bacteria. The knowledge may also be a factor for the successful application of nisin. Therefore, this review focuses on presenting these two aspects of nisin.

Keywords: Bacteriocin, Lactococcus lactis, lanbiotic, nisin

Full Text:


Nisin is the antimcirobial peptide produced by Lactococcus lactis subsp. Lactis1 . It is the only bacterioicin that have been legally approved as safe for use in food and beverage. Nisin was first commercially marketed in England in 1953. In 1969, a joint commission between the Food and Agriculture Organization of the United Nation (FAO) and The World Health Organization (WHO) recognized nisin as a safe and legal biological food preservative. In the United States, the use of nisin in food has been legally approved by the American Food and Drug Administration (FDA) since 19882 . The word “nisin” (Group N Inhibitory Substance + the suffix “in”) was coined by Mattick and Hirsch3 to distinguish nisin from the bacteriocin produced by Lactococcus lactis subsp. cremoris called diplococcin. Nisin is a heat stable, cationic lantibiotic belonging to class I bacteriocin according to the classification criteria of Klaenhammer4 . It consists of 34 amino acids. Of these amino acids, there are several unusual amino acids including dehydroalanine (Dha), dehydrobutyrine (Dhb), aminobutyric acid (Aba), lanthionine (Ala-S-Ala) and β-methyllanthionine (Aba-S-Ala). Nisin has antimicrobial activity against many species of Gram positive bacteria (Table 1), but not Gram negative bacteria due to their outer membrane barrier. Normally, nisin producer has immunity to its own produced nisin but not to other lantibotics. This is for protecting itself from being killed by its own nisin. Although it is a protein, it is not digested by all of the protein digesting enzymes. It is sensitive to chymotrypsin, but not to trypsin and pronase5 . At present, several natural nisin variants have been reported including nisin A1 , nisin Z6 , nisin Q7 , nisin F8 , nisin U8 and nisin U28 . Nisin A, nisin Z, nisin Q and nisin F are produced by Lactococcous lactis while nisin U and nisin U2 produced by Streptococcus sp.8 Of the bacteriocins, only nisin A and nisin Z have been extensively studied. These variants differ in a single amino acid residue at position 27 which is histidine in nisin A and aspartic acid in nisin Z.


Nisin is ribosomally produced from a structural gene as a prenisin having 57 amino acids (Fig. 1 A). It is an inactive form of nisin containing a leader peptide (having 23 amino acids) at the N terminus of the molecule. Modifications after nisin synthesis are dehydration (Fig. 1 B), cyclization (Fig. 1 C) and leader peptide digestion (Fig. 1 D). In the dehydration step, serine and threonine are dehydrated to dehydroalanine (Dha) and dehydrobutyrine (Dhb), respectively. In cyclization step, several thioether crosslinks (S) are formed between alanine and alanine and between aminobutyric acid and alanine. The thioether crosslink between alanine and alanine results in the formation of lanthionine (A-S-A) and that between aminobutyric acid (Abu) and alanine results in the formation of β-methyllanthionine (Abu-S-A). Upon export of nisin outside the cell, leader peptide is digested from the prenisin resulting in the active nisin that is containing 34 amino acids.


For its killing activity, nisin does not require a membrane receptor on its target cell. This is unlike killing activity of many bacteriocins such as colicin that need membrane receptors on target cells. There are two major steps for nisin to kill sensitive cells. 1. Passage through cell wall To pass through target cell wall, nisin generally interactions (via hydrophobic or electrostatic interactions) with anionic components in the cell wall of sensitive cells such as teichoic acids, teichuronic acids and lipoteichoic acids, acidic polysaccharides or phospholipids9 . 2. Interaction with lipid II Lipid II (Fig. 2) is a membrane anchored cell wall precursor that is essential for bacterial cell wall biosynthesis. It is composed of a membrane anchor of 11 polyisoprene residues to which, via a pyrophosphate, the basic building block of the cell wall (peptidoglycan monomer), Nacetylglucosamine-N-acetylmuramic acid(pentapeptide), is attached. It brings the peptidoglycan monomer from cytoplasm of the bacterial cell to incorporate into growing peptidoglycan network in the bacterial cell wall (Fig. 3).

Once nisin reaches cell membrane of the sensitive cells, it may perform one of these actions. 2.1. It binds to lipid II and prevents the peptidoglycan monomer to incorporation into the growing peptidoglycan network (Fig. 4).

2.2. It uses N-terminal binding motif to bind to the carbohydrate-pyrophosphate moiety of lipid II. This enables the C-terminal segment of nisin to insert into the cell membrane. Several nisin-lipid II complexes assemble to form a stable pore with diameter of 2 nanometers in cell membrane of target cells (Fig. 5)10. However, some reports state that the pore is formed by 4 nisin-lipid II complex and 4 nisin molecules (Fig. 6). Once the pore is formed in cell membrane, it can cause an increase in membrane permeability which can lead to the dissipation of the membrane potential, an efflux of small cytoplasmic contents such as amino acids, nucleotides and ions from the damaged cells11,12. Consequently, the damaged cells cannot produce energy as well as vital macromolecules resulting in cell death eventually11,13.

Besides the lipid II mediated mode of action, nisin can cause lysis of the cell wall of sensitive cells (Fig. 7), particularly in staphylococci.

Inhibition of Gram negative bacteria by nisin together with other treatments As mentioned earlier, nisin has antimicrobial activity against some Gram positive bacteria but not against Gram negative bacteria because of their outer membrane barriers. However, many research works show that nisin can inhibit Gram negative bacteria when it is used in combination with substances or physical treatments that destabilize their outer membranes. Table 2 shows some examples of antimicrobial activity of nisin together with other substances or treatments against a variety of Gram negative bacteria both in vitro and in foods.


Although the production and posttranslational modification of Nisin are now fully understood, its mechanism of antimicrobial action still requires further investigation. This may be because nisin has more than one mechanisms of antimicrobial action depending on several factors such as structural properties of target bacteria. Nisin, by itself, is only active against Gram positive bacteria. However, the use of Nisin together with outer membrane destabilizing treatments makes it become active against Gram negative bacteria. This finding broadens the application of Nisin as a food preservative


Authors acknowledge the immense help received from the scholars whose articles are cited and included in references of this manuscript. The authors are also grateful to authors / editors /publishers of all those articles, journals and books from where the literature for this article has been reviewed and discussed.

Source of funding: The Faculty of Science, Ubon Ratchathani University, Thailand

Conflict of Interest: The authors declare that there is no conflict of interest regarding the publication of this article


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