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Bacterial peptide, also known as bacteriocin, is generally defined as a multifunctional peptide synthesized in microbial ribosomes that has antimicrobial activity at a certain concentration. In 1925, bacteriocin in colibacillus was first reported by Grecia. To date, more than 1,700 bacterial peptides have been discovered. These bacterial peptides can be obtained from animals, plants, bacteria or artificial synthesis. The genes encoding bacterial peptides are mainly located on plasmids, and some are located on chromosomes and transposons, which must be transcribed and translated to be biologically active. Since bacterial peptide is essentially a kind of protein, when it is ingested into the human body, it will be gradually decomposed by pepsin. Therefore, bacterial peptide will not accumulate in the body and cause harm to human health.
Among the bacterial peptide, the mechanism of nisin has been deeply studied. There are two main mechanisms of inhibition: one is to form pores on the cell membrane, and the other is to inhibit the synthesis of cell walls to inhibit the growth of bacteria. It is reported that nisin acts on Staphylococcus cohnii 22 and causes cations such as ATP and K+ to flow out of cells, which causes loss of membrane potential and inhibiting growth of bacteria. The loss of intracellular material results from the formation of pores by nisin acting on the cell membrane.
As a natural, highly effective and non-toxic biological preservative, bacterial peptide is of great significance to the development of the food industry. At present, only nisin is used in the food industry. For example, nisin has been added to cheese, cream, pasteurized milk, canned vegetables, alcoholic beverages and other products for preservation. However, nisin has a narrow spectrum of inhibition and limited effect, which cannot fully meet the needs of the development of the food industry. Therefore, the exploration of a new type of bacterial peptide with a broad spectrum of inhibition is the next major research spot.
References
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