Table 2.

Classification of bacteriocins

Class	Nomenclature	Qualities	Examples	Reference
Class-I	Post-translationally modified peptides called Lantibiotics	Characterized by distinctive thioether-based intramolecular rings of lanthionine and β-methyl-lanthionine	Nisin, discovered in 1928, lacticin L. lactis, citolysin of E. faecalis, and lacticin of L. lactis	Xie and van der Donk, 2004
Class-II	Thermostable, non-modified non-lantibiotic linear peptides of <10 kDa. It is recognized as largest class among Gram positive bacteriocins and further divided into three subclasses based on distinctive N-terminal sequence. i. Class II-1-Pediocin-like bacteriocins ii. Class II-2 lacks leader peptide iii. Class II-3 other than above.	Characterized By short cationic peptides with high isoelectric points. It contains potent-antilisteria activity	Pediocin PA-1/AcH produced by Pediococcus, Enterocin EJ97 by E. faecalis and Enterocin L50A by E. faecalis.	Breukink et. al., 1999
Class-III	Comprises large (> 30 KDa) heat labile proteins like colicin- V and microcins.	Bacteriocins are Gram negative circular peptides characterized by a peptide bond between the C- and N-terminus. It possesses the bacteriolytic extracellular enzymes like hemolysins and muramidases which can mimic the physiological activities of bacteriocins.	Helveticin J of L. helveticus and bacteriocin Bc-48 of E. faecalis.	Wiedemann et al., 2001
Class-IV	Circular peptides posses intriguing and novel type of antimicrobial substances produced not only by bacteria but also by plants and mammalian cells.	Characterized by a peptide bond between the C- and N-terminus are clustered. They are existed in form of head-to-tail peptide chain ligation, which makes thermmolecules with neither an origin nor an end.	Enterocin AS-48	Martínez et al., 2008