Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som)
A total of 48 lactic acid bacteria (LAB) exhibited antagonistic activity against Lactobacillus sakei subsp. sakei JCM 1157 or Staphylococcus aureus DMST 8840. Only strain K2N7 was selected for characterization of bacteriocin activity. It was identified as Lactobacillus pentosus based on 16S rDNA a...
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Prince of Songkla University
2016-02-01
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Series: | Songklanakarin Journal of Science and Technology (SJST) |
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Online Access: | http://rdo.psu.ac.th/sjstweb/journal/38-1/38-1-7.pdf |
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author | Nisit Watthanasakphuban Akio Tani Soottawat Benjakul Suppasil Maneerat |
author_facet | Nisit Watthanasakphuban Akio Tani Soottawat Benjakul Suppasil Maneerat |
author_sort | Nisit Watthanasakphuban |
collection | DOAJ |
description | A total of 48 lactic acid bacteria (LAB) exhibited antagonistic activity against Lactobacillus sakei subsp. sakei JCM
1157 or Staphylococcus aureus DMST 8840. Only strain K2N7 was selected for characterization of bacteriocin activity. It was
identified as Lactobacillus pentosus based on 16S rDNA analysis. The maximum bacteriocin production was detected in
early stationary phase of growth. It was found to be sensitive to proteolytic enzymes (trypsin, proteinase K, pronase E and
-chymotrypsin). The bacteriocin K2N7 was heat stable (2 h at 100ºC) and retained activity over a wide pH range (2.0-12.0).
Bacteriocin K2N7 has a narrow inhibitory spectrum restricted to genus Lactobacillus including Lactobacillus plantarum
D6SM3, a bacterial strain known to cause overfermentation in Kung-Som. The peptide was purified by 60% ammonium
sulphate precipitation followed by sequential cation exchange chromatography and hydrophobic interaction characteristic.
The molecular mass of bacteriocin K2N7 (2.017 kDa) was determined by matrix-assisted laser desorption/ionization time-offlight
mass spectrometry analysis (MALDI-TOF MS). |
first_indexed | 2024-12-10T05:19:50Z |
format | Article |
id | doaj.art-f1665c3d47374967a063fa5a4d33e38d |
institution | Directory Open Access Journal |
issn | 0125-3395 |
language | English |
last_indexed | 2024-12-10T05:19:50Z |
publishDate | 2016-02-01 |
publisher | Prince of Songkla University |
record_format | Article |
series | Songklanakarin Journal of Science and Technology (SJST) |
spelling | doaj.art-f1665c3d47374967a063fa5a4d33e38d2022-12-22T02:00:51ZengPrince of Songkla UniversitySongklanakarin Journal of Science and Technology (SJST)0125-33952016-02-013814755Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som)Nisit Watthanasakphuban0Akio Tani1Soottawat Benjakul2Suppasil Maneerat3Department of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112 Thailand.Institute of Plant Science and Resources, Okayama University, Japan.Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112 Thailand.Department of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112 Thailand.A total of 48 lactic acid bacteria (LAB) exhibited antagonistic activity against Lactobacillus sakei subsp. sakei JCM 1157 or Staphylococcus aureus DMST 8840. Only strain K2N7 was selected for characterization of bacteriocin activity. It was identified as Lactobacillus pentosus based on 16S rDNA analysis. The maximum bacteriocin production was detected in early stationary phase of growth. It was found to be sensitive to proteolytic enzymes (trypsin, proteinase K, pronase E and -chymotrypsin). The bacteriocin K2N7 was heat stable (2 h at 100ºC) and retained activity over a wide pH range (2.0-12.0). Bacteriocin K2N7 has a narrow inhibitory spectrum restricted to genus Lactobacillus including Lactobacillus plantarum D6SM3, a bacterial strain known to cause overfermentation in Kung-Som. The peptide was purified by 60% ammonium sulphate precipitation followed by sequential cation exchange chromatography and hydrophobic interaction characteristic. The molecular mass of bacteriocin K2N7 (2.017 kDa) was determined by matrix-assisted laser desorption/ionization time-offlight mass spectrometry analysis (MALDI-TOF MS).http://rdo.psu.ac.th/sjstweb/journal/38-1/38-1-7.pdfbacteriocinKung-Somfermented shrimpnarrow spectrumLactobacillus pentosus |
spellingShingle | Nisit Watthanasakphuban Akio Tani Soottawat Benjakul Suppasil Maneerat Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) Songklanakarin Journal of Science and Technology (SJST) bacteriocin Kung-Som fermented shrimp narrow spectrum Lactobacillus pentosus |
title | Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) |
title_full | Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) |
title_fullStr | Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) |
title_full_unstemmed | Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) |
title_short | Detection and preliminary characterization of a narrow spectrum bacteriocin produced by Lactobacillus pentosus K2N7 from Thai traditional fermented shrimp (Kung-Som) |
title_sort | detection and preliminary characterization of a narrow spectrum bacteriocin produced by lactobacillus pentosus k2n7 from thai traditional fermented shrimp kung som |
topic | bacteriocin Kung-Som fermented shrimp narrow spectrum Lactobacillus pentosus |
url | http://rdo.psu.ac.th/sjstweb/journal/38-1/38-1-7.pdf |
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