Purification and characterization of a novel plantaricin, KL-1Y, from Lactobacillus plantarum KL-1

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• 作者：Kittaporn Rumjuankiat ; Rodney Horanda Perez…
• 关键词：Bacteriocin ; Lactobacillus plantarum ; Purification ; Characterization ; Synergism ; Bactericidal activity
• 刊名：World Journal of Microbiology & Biotechnology
• 出版年：2015
• 出版时间：June 2015
• 年：2015
• 卷：31
• 期：6
• 页码：983-994
• 全文大小：682 KB
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• 作者单位：Kittaporn Rumjuankiat (1)
  Rodney Horanda Perez (3)
  Komkhae Pilasombut (4)
  Suttipun Keawsompong (1) (2)
  Takeshi Zendo (3)
  Kenji Sonomoto (3) (5)
  Sunee Nitisinprasert (1) (2)
  
  1. Specialized Research Unit: Prebiotics and Probiotics for Health, Department of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Lat Yao, Chatuchak, Bangkok, 10900, Thailand
  3. Laboratory of Microbial Technology, Division of Systems Bioengineering, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Higashi-ku, Fukuoka, Japan
  4. Department of Animal Production Technology and Fisheries, Faculty of Agricultural Technology, King Mongkut’s Institute of Technology Ladkrabang, Bangkok, 10520, Thailand
  2. Center for Advanced Studies for Agriculture and Food, (CASAF) Kasetsart University Institute for Advanced Studies (NRU-KU), Kasetsart University, Chatuchak, Bangkok, 10900, Thailand
  5. Laboratory of Functional Food Design, Department of Functional Metabolic Design, Bio-Architecture Center, Kyushu University, Higashi-ku, Fukuoka, Japan
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Applied Microbiology
  Biotechnology
  Biochemistry
  Environmental Biotechnology
  Microbiology
  
• 出版者：Springer Netherlands
• ISSN：1573-0972

文摘

Three bacteriocins from Lactobacillus plantarum KL-1 were successfully purified using ammonium sulfate precipitation, cation-exchange chromatography and reverse-phase HPLC. The bacteriocin peptides KL-1X, -1Y and -1Z had molecular masses of 3053.82, 3498.16 and 3533.16?Da, respectively. All three peptides were stable at pH 2-2 and 25?°C and at high temperatures of 80 and 100?°C for 30?min and 121?°C for 15?min. However, they differed in their susceptibility to proteolytic enzymes and their inhibition spectra. KL-1Y showed broad inhibitory activities against Gram-positive and Gram-negative bacteria, including Salmonella enterica serovar Enteritidis DMST 17368, Pseudomonas aeruginosa ATCC 15442, P. aeruginosa ATCC 9027, Escherichia coli O157:H7 and E. coli ATCC 8739. KL-1X and -1Z inhibited only Gram-positive bacteria. KL-1X, KL-1Y and KL-1Z exhibited synergistic activity. The successful amino acid sequencing of KL-1Y had a hydrophobicity of approximately 30?% and no cysteine residues suggested its novelty, and it was designated “plantaricin KL-1Y- Plantaricin KL-1Y exhibited bactericidal activity against Bacillus cereus JCM 2152T. Compared to nisin, KL-1Y displayed broad inhibitory activities of 200, 800, 1600, 800, 400 and 400?AU/mL against the growth of Bacillus coagulans JCM 2257T, B. cereus JCM 2152T, Listeria innocua ATCC 33090T, Staphylococcus aureus TISTR 118, E. coli O157:H7 and E. coli ATCC 8739, respectively, whereas nisin had similar activities against only B. coagulans JCM 2257T and B. cereus JCM 2152T. Therefore, the novel plantaricin KL-1Y is a promising antimicrobial substance for food safety uses in the future.