Identification of an anti-listerial domain from Pediococcus pentosaceus T1 derived from Kimchi, a traditional fermented vegetable

Seongho Jang, Joohyung Lee, Uisub Jung, Hyeon Son Choi, Hyung Joo Suh

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The aim of this study was to isolate and identify anti-listerial substances produced by lactic acid bacteria in Kimchi, a traditional fermented vegetable. The Pediococcus pentosaceus T1 strain, which has an antimicrobial effect on Listeria monocytogenes, was isolated from Kimchi using 16S rRNA analysis. A crude culture of P.pentosaceus T1 demonstrated anti-listerial activity that was unaltered by pH changes in the range of 4-8 and temperatures between 80 and 110°C. However, anti-listerial activity of P.pentosaceus T1 was abolished upon protease- and lipase-treatments, suggesting that the active substances were composed of peptides and lipids. Amylase, however, showed very little change in activity when compared to the control. Passage of the culture supernatant over Sep-Pak C18 cartridges showed that the anti-listerial activity could be traced to a component in the water-soluble fraction. Further purification of the activity was carried out using a series of steps that included ammonium sulfate precipitation, desalting, ion exchange chromatography, and ultrafiltration of the supernatants of P.pentosaceus cultures. The active fraction showed the presence of a 23-kDa protein, as visualized by SDS-PAGE followed by coomassie blue staining. Liquid chromatography (LC) and mass spectrometry (MS) analyses of the protein confirmed the presence of a Lysin motif (LysM) domain, which is known to be present in bacterial peptidoglycan hydrolases. In this study, we have demonstrated that Kimchi-derived P.pentosaceus shows an anti-listerial activity, and identified the active moiety as a LysM domain in a 23-kDa protein.

Original languageEnglish
Pages (from-to)42-48
Number of pages7
JournalFood Control
Volume43
DOIs
Publication statusPublished - 2014 Sep 1

Fingerprint

kimchi
Pediococcus pentosaceus
Vegetables
vegetables
N-acetylmuramoyl-L-alanine amidase
N-Acetylmuramoyl-L-alanine Amidase
Proteins
proteins
Ion Exchange Chromatography
Ultrafiltration
Ammonium Sulfate
Listeria monocytogenes
anti-infective properties
ion exchange chromatography
Amylases
ultrafiltration
Lipase
amylases
ammonium sulfate
Liquid Chromatography

Keywords

  • Anti-listerial activity
  • Kimchi
  • Lysin motif domain
  • Pediococcus pentosaceus T1

ASJC Scopus subject areas

  • Food Science
  • Biotechnology

Cite this

Identification of an anti-listerial domain from Pediococcus pentosaceus T1 derived from Kimchi, a traditional fermented vegetable. / Jang, Seongho; Lee, Joohyung; Jung, Uisub; Choi, Hyeon Son; Suh, Hyung Joo.

In: Food Control, Vol. 43, 01.09.2014, p. 42-48.

Research output: Contribution to journalArticle

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abstract = "The aim of this study was to isolate and identify anti-listerial substances produced by lactic acid bacteria in Kimchi, a traditional fermented vegetable. The Pediococcus pentosaceus T1 strain, which has an antimicrobial effect on Listeria monocytogenes, was isolated from Kimchi using 16S rRNA analysis. A crude culture of P.pentosaceus T1 demonstrated anti-listerial activity that was unaltered by pH changes in the range of 4-8 and temperatures between 80 and 110°C. However, anti-listerial activity of P.pentosaceus T1 was abolished upon protease- and lipase-treatments, suggesting that the active substances were composed of peptides and lipids. Amylase, however, showed very little change in activity when compared to the control. Passage of the culture supernatant over Sep-Pak C18 cartridges showed that the anti-listerial activity could be traced to a component in the water-soluble fraction. Further purification of the activity was carried out using a series of steps that included ammonium sulfate precipitation, desalting, ion exchange chromatography, and ultrafiltration of the supernatants of P.pentosaceus cultures. The active fraction showed the presence of a 23-kDa protein, as visualized by SDS-PAGE followed by coomassie blue staining. Liquid chromatography (LC) and mass spectrometry (MS) analyses of the protein confirmed the presence of a Lysin motif (LysM) domain, which is known to be present in bacterial peptidoglycan hydrolases. In this study, we have demonstrated that Kimchi-derived P.pentosaceus shows an anti-listerial activity, and identified the active moiety as a LysM domain in a 23-kDa protein.",
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