Purification and characterization of thermophilin ST-1, a novel bacteriocin produced by Streptococcus thermophilus ACA-DC 0001

dc.contributor.author	Aktypis, A	en
dc.contributor.author	Kalantzopoulos, G	en
dc.date.accessioned	2014-06-06T06:45:35Z
dc.date.available	2014-06-06T06:45:35Z
dc.date.issued	2003	en
dc.identifier.issn	00237302	en
dc.identifier.uri	http://dx.doi.org/10.1051/lait:2003024	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/2526
dc.subject	Antimicrobial activity	en
dc.subject	Bacteriocin	en
dc.subject	Lactic acid bacteria	en
dc.subject	Phytopathogen	en
dc.subject	Streptococcus thermophilus	en
dc.subject	Thermophilin	en
dc.subject.other	Chromosomes	en
dc.subject.other	Enzymes	en
dc.subject.other	Precipitation (chemical)	en
dc.subject.other	Purification	en
dc.subject.other	Size exclusion chromatography	en
dc.subject.other	Food spoilage	en
dc.subject.other	Bacteria	en
dc.subject.other	Enterococcus faecalis	en
dc.subject.other	Erwinia	en
dc.subject.other	Lactococcus lactis	en
dc.subject.other	Listeria innocua	en
dc.subject.other	Negibacteria	en
dc.subject.other	Pseudomonas	en
dc.subject.other	Pseudomonas syringae	en
dc.subject.other	Staphylococcus aureus	en
dc.subject.other	Streptococcus thermophilus	en
dc.subject.other	Xanthomonas campestris	en
dc.title	Purification and characterization of thermophilin ST-1, a novel bacteriocin produced by Streptococcus thermophilus ACA-DC 0001	en
heal.type	journalArticle	en
heal.identifier.primary	10.1051/lait:2003024	en
heal.publicationDate	2003	en
heal.abstract	Thermophilin ST-1 is produced by Streptococcus thermophilus ACA-DC 0001, a ""wild"" strain isolated from traditional Greek yogurt products. It exerts an inhibitory effect on lactic acid bacteria, several food spoilage and food-borne pathogenic microorganisms, and some Gram-negative phytopathogen bacteria, including Listeria innocua BL 86/20, Enterococcus faecalis EF1, Staphylococcus aureus ATCC 29996, Xanthomonas campestris BPIC 1660, Pseudomonas syringae EPIC 1549 and Erwinia rubrifasciens BPIC 1710. The crude antimicrobial compound is heat-labile (60 °C for 10 min) and sensitive to the proteolytic enzymes pronase and trypsin and high acidic and alkaline conditions, and shows a bactericidal mode of action against the indicator strain Lactococcus lactis ssp. cremoris CNRZ-117. Production of thermophilin ST-1 starts during the early growth of the producer strain and reaches a maximum titer of 2560 AU·mL-1 at the end of the exponential growth. Thermophilin ST-1 was partially purified by ammonium sulfate precipitation, ion-exchange and size-exclusion chromatography. SDS-PAGE electrophoresis of purified thermophilin ST-1 showed a single protein band with a molecular mass of 30 kg·mol-1, classifying this novel bacteriocin with the large heat-labile proteins. Until now, however, the molecular mass of bacteriocins reported in the species of S. thermophilus was less than 10 kg·mol -1 (small, heat-stable peptides). Curing experiments did not result in the loss of bacteriocin production, suggesting that the genetic determinant is probably located on the chromosome.	en
heal.journalName	Lait	en
dc.identifier.issue	5	en
dc.identifier.volume	83	en
dc.identifier.doi	10.1051/lait:2003024	en
dc.identifier.spage	365	en
dc.identifier.epage	378	en