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논문 기본 정보

자료유형
학술저널
저자정보
홍성욱 (세계김치연구소) Kim Jong-Hui (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) Cha Hyun A (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) 정건섭 (연세대학교) Bae Hyo Ju (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) Park Won Seo (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) Ham Jun-Sang (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) Park Beom-Young (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea) Oh Mi-Hwa (National Institute of Animal Science Rural Development Administration Wanju 55365 Republic of Korea)
저널정보
한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제32권 제11호
발행연도
2022.11
수록면
1,462 - 1,470 (9page)
DOI
10.4014/jmb.2208.08006

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Natural antimicrobial substances are needed as alternatives to synthetic antimicrobials to protect against foodborne pathogens. In this study, a bacteriocin-producing bacterium, Bacillus subtilis HD15, was isolated from doenjang, a traditional Korean fermented soybean paste. We sequenced the complete genome of B. subtilis HD15. This genome size was 4,173,431 bp with a G + C content of of 43.58%, 4,305 genes, and 4,222 protein-coding genes with predicted functions, including a subtilosin A gene cluster. The bacteriocin was purified by ammonium sulfate precipitation, Diethylaminoethanol-Sepharose chromatography, and Sephacryl gel filtration, with 12.4-fold purification and 26.2% yield, respectively. The purified protein had a molecular weight of 3.6 kDa. The N-terminal amino acid sequence showed the highest similarity to Bacillus subtilis 168 subtilosin A (78%) but only 68% similarity to B. tequilensis subtilosin proteins, indicating that the antimicrobial substance isolated from B. subtilis HD15 is a novel bacteriocin related to subtilosin A. The purified protein from B. subtilis HD15 exhibited high antimicrobial activity against Listeria monocytogenes and Bacillus cereus. It showed stable activity in the range 0–70°C and pH 2–10 and was completely inhibited by protease, proteinase K, and pronase E treatment, suggesting that it is a proteinaceous substance. These findings support the potential industrial applications of the novel bacteriocin purified from B. subtilis HD15.

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