Nisin: 100 years of research on the food preservative
What it found
Nisin is a peptide made by bacteria that kills other bacteria.
Over the last century it has been used as a food preservative and studied for possible medical uses.
What they found
Animal and lab studies
How nisin kills bacteria
Nisin binds to lipid II, a building block of the bacterial cell wall, and also forms pores in the bacterial membrane. This dual action makes it potent against many Gram-positive bacteria.
Resistance to nisin
Some bacteria, including human pathogens, carry genes that give them resistance to nisin. These resistance genes are sometimes on mobile pieces of DNA that can be passed between bacteria.
New nisin variants
Many new natural nisin variants have been found in human, animal, and insect microbiomes. Some of these variants have different activity against bacteria compared to the original nisin.
Engineered nisin
Scientists have made hundreds of modified versions of nisin in the lab. Some of these have better activity against harmful bacteria or can avoid resistance mechanisms.
Nisin and gut bacteria
Nisin can affect the gut microbiome, and some nisin-producing bacteria in the gut may help compete against harmful microbes. This has led to interest in using nisin to shape the gut microbiome.
Other findings
How nisin is made
Nisin is first made as a longer precursor peptide that is then modified by enzymes inside the bacterial cell. The modified peptide is exported and the leader portion is cut off to release the active nisin.
What the authors conclude
“If nisin is to achieve more widespread therapeutic use, it is critical that resistance be taken into consideration at every stage of development.”
Also in their conclusions
- They say that nisin has been a paradigm for understanding lantibiotic biosynthesis and has found success as a food preservative.
- They note that new natural variants and bioengineered derivatives offer exciting prospects for therapeutic applications.
- They stress that if nisin is to achieve more widespread therapeutic use, it is critical that resistance be taken into consideration at every stage of development.
How it was done
The authors wanted to mark almost a century since nisin was discovered and to review the latest progress in understanding how it is made, how bacteria resist it, and how it might be used in medicine.
They reviewed the scientific literature on nisin, covering its discovery, how it is made by bacteria, how bacteria become resistant to it, new natural variants found in human and animal guts, and efforts to engineer new versions.
What it can’t tell you
- This is a review of laboratory and animal studies. It cannot show what happens when people eat nisin or take it as a medicine.
- The paper does not report on clinical trials in people, so it cannot say whether nisin is effective or safe for human health.
- The findings on resistance and new variants come from lab experiments and may not predict how bacteria behave in the human body.
Who paid
- Funding
- Funded by Science Foundation Ireland (from the PubMed record).
- Conflicts
- None declared.
- Authors work at
- University College Cork, Ireland
The paper
- Title
- After a century of nisin research - where are we now?
- Type
- ReviewThe authors read earlier studies and describe what they found. It isn’t a new study.
- Evidence
- Animals and lab studies
- Summarised from
- Full text
- Cite
- Field D, Fernandez de Ullivarri M, Ross RP, Hill C (2023). After a century of nisin research - where are we now?. FEMS microbiology reviews. doi:10.1093/femsre/fuad023Free full textPubMed 37300874DOI
Summary written 26 Sep 2026. Check it against the paper before it changes what you eat. How we summarise papers · Report an error