Biosynthesis of nisin, antimicrobial mechanism and its applications as a food preservation: A review

Abstract

Abstract This review examines the biosynthesis of nisin, its antimicrobial mechanism, and its applications in food preservation. Nisin is synthesized withinside the ribosome as a pre-peptide which undergoes amendment withinside the post-translational level as a number one metabolite from lactic acid bacteria. Nisin secretion occurs in the exponential phase and is maximally produced at the end of the exponential phase or the beginning of the stationary phase. As an antibiotic in the form of a peptide molecule, nisin is characterized by the presence of lanthionine-type thioester bonds. Nisin has been reported to have the ability to inhibit bacteria, especially Gram-positive bacteria such as Bacillus subtilis, Bacillus stearothermophilus, Clostridium botulinum, Streptococcus hemolyticus, Staphylococcus aureus, and Listeria monocytogenes. Nevertheless, nisin is less effective against Gram-negative bacteria, yeast, and molds. Based on its ability to inhibit bacteria plus the non-toxic nature of nisin, Nisin can be used as bio preservation in food products. Besides being non-toxic, several other factors that can be considered for nisin as bio preservation are that nisin is readily biodegradable. It is a protein compound that does not harm the intestinal flora as it is easily digested by enzymes in the gastrointestinal tract and does not cause bacterial resistance as therapeutic antibiotics are safe for humans.