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Characterization of bacteriocins from two Lactococcus lactis subsp. lactis isolates

✍ Scribed by Oya Akçelik; Çaǧla Tükel; Gülay Özcengiz; Mustafa Akçelik

Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
952 KB
Volume
50
Category
Article
ISSN
1613-4125

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✦ Synopsis

Abstract

In this study, bacteriocins from two Lactococcus lactis subsp. lactis isolates from raw milk samples in Turkey designated OC1 and OC2, respectively, were characterized and identified. The activity spectra of the bacteriocins were determined by using different indicator bacteria including Listeria, Bacillus and Staphylococcus spp. Bacteriocins were tested for their sensitivity to different enzymes, heat treatments and pH values. Loss of bacteriocin activities after α‐amylase treatment suggested that they form aggregates with carbohydrates. Molecular masses of the purified bacteriocins were determined by SDS‐PAGE. PCR amplification was carried out with specific primers for the detection of their structural genes. As a result of these studies, the two bacteriocins were characterized as nisin and lacticin 481, respectively. Examination of plasmid contents of the isolates and the results of plasmid curing and conjugation experiments showed that in L. lactis subsp. lactis OC1 strain the 39.7‐kb plasmid is responsible for nisin production, lactose fermentation and proteolytic activity, whereas the 16.0‐kb plasmid is responsible for lacticin 481 production and lactose fermentation in L. lactis subsp. lactis OC2 strain.

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