Heterologous expression of gassericin A, a bacteriocin produced by Lactobacillus gasseri LA39

Yasushi Kawai, Kensuke Arakawa, Ayako Itoh, Boku Saitoh, Yasuyuki Ishii, Junko Nishimura, Haruki Kitazawa, Takatoshi Itoh, Tadao Saito

    研究成果: Article査読

    15 被引用数 (Scopus)

    抄録

    Gassericin A, a bacteriocin produced by Lactobacillus gasseri LA39, has a cyclic structure linking N- and C-terminal amino acids. Gassericin A was expressed in Escherichia coli JM109 as a biotinylated fusion protein on the basis of the DNA sequence of mature bacteriocin. A positive clone accumulated the bacteriocin, with no activity, as a soluble fusion protein in the cytoplasm. After release of an N-terminal tag with factor Xa protease, gassericin A was converted into an active peptide having N- and C-termini. The total amount of purified bacteriocins (expressed and native) was 480 μg/L and 370 μg/L, respectively. However, the specific activity of expressed gassericin A was 15 AU/mg lower than that of native bacteriocin (2600 AU/mg). Although the actual Mr (molecular weight) of the expressed bacteriocin should be 5666, the peptide showed the same mobility (Mr 3800) in sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as native cyclic gassericin A, suggesting that the expressed peptide retains compact folding of the molecule similar to that of native gassericin A.

    本文言語English
    ページ(範囲)45-51
    ページ数7
    ジャーナルAnimal Science Journal
    74
    1
    DOI
    出版ステータスPublished - 2003 2月 1

    ASJC Scopus subject areas

    • 農業および生物科学(全般)

    フィンガープリント

    「Heterologous expression of gassericin A, a bacteriocin produced by Lactobacillus gasseri LA39」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

    引用スタイル