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タイトル: | Enzyme systems involved in glucosinolate metabolism in Companilactobacillus farciminis KB1089 |
著者: | Watanabe, Hiroko Usami, Riku Kishino, Shigenobu ![]() ![]() ![]() Osada, Kengo Aoki, Yudai Morisaka, Hironobu Takahashi, Masatomo Izumi, Yoshihiro Bamba, Takeshi Aoki, Wataru ![]() ![]() Suganuma, Hiroyuki Ogawa, Jun ![]() ![]() ![]() |
著者名の別形: | 渡邊, 寛子 岸野, 重信 森坂, 裕信 青木, 航 小川, 順 |
キーワード: | Applied microbiology Bacteria |
発行日: | 2021 |
出版者: | Springer Nature |
誌名: | Scientific Reports |
巻: | 11 |
論文番号: | 23715 |
抄録: | Cruciferous vegetables are rich sources of glucosinolates (GSLs). GSLs are degraded into isothiocyanates, which are potent anticarcinogens, by human gut bacteria. However, the mechanisms and enzymes involved in gut bacteria-mediated GSL metabolism are currently unclear. This study aimed to elucidate the enzymes involved in GSL metabolism in lactic acid bacteria, a type of gut bacteria. Companilactobacillus farciminis KB1089 was selected as a lactic acid bacteria strain model that metabolizes sinigrin, which is a GSL, into allylisothiocyanate. The sinigrin-metabolizing activity of this strain is induced under glucose-absent and sinigrin-present conditions. A quantitative comparative proteomic analysis was conducted and a total of 20 proteins that were specifically expressed in the induced cells were identified. Three candidate proteins, β-glucoside-specific IIB, IIC, IIA phosphotransferase system (PTS) components (CfPttS), 6-phospho-β-glucosidase (CfPbgS) and a hypothetical protein (CfNukS), were suspected to be involved in sinigrin-metabolism and were thus investigated further. We hypothesize a pathway for sinigrin degradation, wherein sinigrin is taken up and phosphorylated by CfPttS, and subsequently, the phosphorylated entity is degraded by CfPbgS. As expression of both pttS and pbgS genes clearly gave Escherichia coli host strain sinigrin converting activity, these genes were suggested to be responsible for sinigrin degradation. Furthermore, heterologous expression analysis using Lactococcus lactis suggested that CfPttS was important for sinigrin degradation and CfPbgS degraded phosphorylated sinigrin. |
著作権等: | Copyright © 2021, The Author(s) Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. |
URI: | http://hdl.handle.net/2433/276834 |
DOI(出版社版): | 10.1038/s41598-021-03064-7 |
PubMed ID: | 34887468 |
出現コレクション: | 学術雑誌掲載論文等 |
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