Biotechnological production of vanillin using immobilized enzymes

Toshiki Furuya*, Mari Kuroiwa, Kuniki Kino

*この研究の対応する著者

    研究成果: Article査読

    45 被引用数 (Scopus)

    抄録

    Vanillin is an important and popular plant flavor, but the amount of this compound available from plant sources is very limited. Biotechnological methods have high potential for vanillin production as an alternative to extraction from plant sources. Here, we report a new approach using immobilized enzymes for the production of vanillin. The recently discovered oxygenase Cso2 has coenzyme-independent catalytic activity for the conversion of isoeugenol and 4-vinylguaiacol to vanillin. Immobilization of Cso2 on Sepabeads EC-EA anion-exchange carrier conferred enhanced operational stability enabling repetitive use. This immobilized Cso2 catalyst allowed 6.8 mg yield of vanillin from isoeugenol through ten reaction cycles at a 1 mL scale. The coenzyme-independent decarboxylase Fdc, which has catalytic activity for the conversion of ferulic acid to 4-vinylguaiacol, was also immobilized on Sepabeads EC-EA. We demonstrated that the immobilized Fdc and Cso2 enabled the cascade synthesis of vanillin from ferulic acid via 4-vinylguaiacol with repetitive use of the catalysts. This study is the first example of biotechnological production of vanillin using immobilized enzymes, a process that provides new possibilities for vanillin production.

    本文言語English
    ページ(範囲)25-28
    ページ数4
    ジャーナルJournal of Biotechnology
    243
    DOI
    出版ステータスPublished - 2017 2月 10

    ASJC Scopus subject areas

    • バイオテクノロジー
    • 応用微生物学とバイオテクノロジー

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