Bacteriocin plasmids ofPediococcus acidilactici

Ray, Supratim; Johnson, M. C.; Ray, Bibek

doi:10.1007/bf01574073

Cited by 56 publications

(62 citation statements)

References 27 publications

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“…There are several reports of plasmidassociated bacteriocin production from lactic acid bacteria [7,19,25], whereas in other cases, bacteriocin production has been linked to chromosomal DNA [14]. The results of this study suggest that the production of thermophilin ST-1 was not associated with a 2.7 kb plasmid, which is harbored in the S. thermophilus ACA-DC strain.…”

Section: Discussionmentioning

confidence: 49%

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

Aktypis

Kalantzopoulos

2003

Lait

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-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 Gramnegative phytopathogen bacteria, including Listeria innocua BL 86/20 , Enterococcus faecalis EF1, Staphylococcus aureus ATCC 29996, Xanthomonas campestris BPIC 1660, Pseudomonas syringae BPIC 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, ionexchange 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. Streptococcus thermophilus

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Section: Discussionmentioning

confidence: 49%

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

Aktypis

Kalantzopoulos

2003

Lait

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“…However, anticlostridial activity has not been reported for any of these bacteriocins, and their inhibitory spectrum appears to be limited to some (often closely related) LAB, except for thermophilin 347, which was active against Listeria monocytogenes. Furthermore, inhibition of clostridia has also been observed for some bacteriocins produced by other LAB, such as acidocin B (ten Brink et al 1994) and pediocins (Daeschel and Klaenhammer 1985 ;Ray et al 1989 ;Kalchayanand 1990).…”

Section: Discussionmentioning

confidence: 93%

Purification and characterization of thermophilin T, a novel bacteriocin produced by Streptococcus thermophilus ACA-DC 0040

et al. 1998

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ACA‐DC 0040 produced an antimicrobial agent, which was named thermophilin T, active against several lactic acid bacteria strains of different species and food spoilage bacteria, such as Clostridium sporogenes C22/10 and Cl. tyrobutyricum NCDO‐1754. The crude antimicrobial compound is sensitive to proteolytic enzymes and α‐amylase, heat‐stable (100 °C for 30 min), resistant to pH exposure at pH 1–12 and demonstrates a bactericidal mode of action against the sensitive strain Lactococcus cremoris CNRZ‐117. The production of bacteriocin was optimized approximately 10‐fold in an aerobic fermenter held at constant pH 5·8 and 6·2. Ultrafiltration experiments with culture supernatant fluids containing the bacteriocin, and further estimation of molecular weight with gel filtration chromatography, revealed that bacteriocin in the native form has a molecular weight in excess of 300 kDa. SDS‐gel electrophoresis of partially purified thermophilin T showed that bacteriocin activity was associated with a protein band of approximately 2·5 kDa molecular mass.

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“…The isolated bacteriocin termophilin T (Aktypis et al, 1998) from S.thermophilus ACA-DC 0040 inhibits both lactic acid bacteria and clostridia. The inhibition of clostridia was also described for acidocin B (tenBring et al, 1994) and pedocins (Daeschel, 1989;Ray et al, 1989). Thermophilin T regulates population dynamics in the yogurt production and hard cheeses.…”

Section: Fig3 the Two-peptide Lantibiotics Described Among Bacilli mentioning

confidence: 85%

Antibacterial peptides from thermophilic bacteria

Mikulı́k¹,

Melčová²,

Zídková³

2017

engineering-journal

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Bacteriocin plasmids ofPediococcus acidilactici

Cited by 56 publications

References 27 publications

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

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

Purification and characterization of thermophilin T, a novel bacteriocin produced by Streptococcus thermophilus ACA-DC 0040

Antibacterial peptides from thermophilic bacteria

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