Bacteriocins used today as food preservative
Bacteriocins are antibacterial proteins produced by bacteria that kill or inhibit the growth of other bacteria. Many lactic acid bacteria produce a high variety of different bacteriocins. Though these bacteriocins are produced by lactic acid bacteria found in numerous fermented and non-fermented foods, Nisin (E234) is currently the most widely bacteriocin as a food preservative.
Many bacteriocins have been characterized biochemically and genetically, and though there is a basic understanding of their structure-function, biosynthesis, and mode of action, many aspects of these compounds are still unknown. Toxicity data exist for only a few bacteriocins, but research and their long-time intentional use strongly suggest that bacteriocins can be safely used.
Without being themselves antibiotics with all the disadvantages like resistance forming behavior in the organism to be protected, bacteriocins have found a broad application in food preservation.
Bacteriocins are clearly distinguishable from Antibiotics.
They can safely and effectively be used to control the growth of target pathogens in food products.
Bacteriocins can be clearly determined by their basis of synthesis, reactivity with the target organisms its anti-microbial spectrum their toxicity and their resistance mechanisms
The immunity of the cell synthesizing the bacteriocin to its product is a phenomenon that distinguishes bacteriocins from antibiotics.
The chemical composition and the physical conditions of food can have a significant influence.
Nisin a widely used bacteriocin is 228 times more soluble at pH 2 than at pH 8.
Regulatory ruling in food:
Bacteriocins are often falsely described as antibiotics. But the use of Antibiotics is limited legally in food applications.
While in the United States antibiotics are prohibited in foods, bacteriocins received the status GRAS (Generally Recognized as Save) already in 1988.
For approval to be granted the bacteriocin must be chemically identified and characterized and its use and efficacy must be shown. The manufacturing process must be described and analytics for quantification and standardization of the peptide must be shown.