Bacteriocin: Difference between revisions
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'''Bacteriocins''' are [[protein]]aceous [[toxin]]s given off by [[bacterium|bacteria]] to inhibit the growth of similar bacterial strain(s). [[E. coli]] bacteriocins are called colicins. | |||
The bacteriocins of [[lactic acid]]-fermenting bacteria are well studied because of the commercial use of these bacteria in the food industry for making dairy products such as cheese. Bacteriocins are classified according to their extent of [[Posttranslational modification|posttranslational modification]]. The [[lantibiotics]] are a class of more extensively modified bacteriocins, also called Class I. Bacteriocins for which [[disulfide bond]]s are the only modification to the peptide are Class II bacteriocins. Most bacteriocins are biologically active single-chain peptides. Some are only active as partners with a second peptide (see Class IIb, below). | |||
[[Nisin]] and epidermin are members of a family of lantibiotics that bind to a [[Cell_wall#Bacterial_cell_walls|cell wall]] precursor lipid component of target bacteria and disrupt cell wall production. The duramycin family of lantibiotics binds phosphoethanolamine in the membranes of its target cells and seem to disrupt several physiological functions. | |||
The action of Class IIa bacteriocins seems to involve disruption of mannose transport into target cells. Class IIb bacteriocins form pores in the membranes of target cells and disrupt the [[Chemiosmotic hypothesis|proton gradient]] of target cells. Other bacteriocins can be grouped together as Class IIc. These have a wide range of effects on membrane permeability, cell wall formation and pheromone actions of target cells. | |||
Bacteriocins are of interest in medicine because they are made by non-[[pathogenic]] bacteria that normally colonize the human body. Loss of these harmless bacteria following [[antibiotic]] use may allow pathogenic bacteria to invade the human body. | |||
To demonstrate their production, technicians stab inoculate multiple strains on separate multiple nutrient [[agar]] [[Petri dish]]es, incubate at 30 °C for 24 hours, overlay each plate with one of the strains (in soft agar), incubate again at 30 °C for 24 hours. After this process, the presence of bacteriocins can be inferred if there are zones of growth inhibition around stabs.<ref>{{cite journal|last=Udhayashree|first=Narayanapillai|coauthors=Duraisamy Senbagam, Balakrishnan Senthilkumar, Kanagaraj Nithya, Ramasamy Gurusamy|date=28 April 2012|title=Production of bacteriocin and their application in food products|url=http://www.apjtb.com/zz/2012s1/79.pdf|journal=Asian Pacific Journal of Tropical Biomedicine|publisher=Elsevier|volume=2|issue=1|pages=406-410|doi=10.1016/S2221-1691(12)60197-X|accessdate=8 November 2013}}</ref> | |||
==Notes== | |||
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Latest revision as of 16:00, 15 July 2024
Bacteriocins are proteinaceous toxins given off by bacteria to inhibit the growth of similar bacterial strain(s). E. coli bacteriocins are called colicins.
The bacteriocins of lactic acid-fermenting bacteria are well studied because of the commercial use of these bacteria in the food industry for making dairy products such as cheese. Bacteriocins are classified according to their extent of posttranslational modification. The lantibiotics are a class of more extensively modified bacteriocins, also called Class I. Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins. Most bacteriocins are biologically active single-chain peptides. Some are only active as partners with a second peptide (see Class IIb, below).
Nisin and epidermin are members of a family of lantibiotics that bind to a cell wall precursor lipid component of target bacteria and disrupt cell wall production. The duramycin family of lantibiotics binds phosphoethanolamine in the membranes of its target cells and seem to disrupt several physiological functions.
The action of Class IIa bacteriocins seems to involve disruption of mannose transport into target cells. Class IIb bacteriocins form pores in the membranes of target cells and disrupt the proton gradient of target cells. Other bacteriocins can be grouped together as Class IIc. These have a wide range of effects on membrane permeability, cell wall formation and pheromone actions of target cells.
Bacteriocins are of interest in medicine because they are made by non-pathogenic bacteria that normally colonize the human body. Loss of these harmless bacteria following antibiotic use may allow pathogenic bacteria to invade the human body.
To demonstrate their production, technicians stab inoculate multiple strains on separate multiple nutrient agar Petri dishes, incubate at 30 °C for 24 hours, overlay each plate with one of the strains (in soft agar), incubate again at 30 °C for 24 hours. After this process, the presence of bacteriocins can be inferred if there are zones of growth inhibition around stabs.[1]
Notes
- ↑ Udhayashree, Narayanapillai; Duraisamy Senbagam, Balakrishnan Senthilkumar, Kanagaraj Nithya, Ramasamy Gurusamy (28 April 2012). "Production of bacteriocin and their application in food products". Asian Pacific Journal of Tropical Biomedicine 2 (1): 406-410. DOI:10.1016/S2221-1691(12)60197-X. Retrieved on 8 November 2013. Research Blogging.