Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes

Muneharu Goto, Chiaki Hatanaka, Kazuya Uezu, Masahiro Goto

    研究成果: ジャーナルへの寄稿学術誌査読

    1 被引用数 (Scopus)

    抄録

    Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.

    本文言語英語
    ページ(範囲)565-567
    ページ数3
    ジャーナルkagaku kogaku ronbunshu
    29
    4
    DOI
    出版ステータス出版済み - 7月 2003

    !!!All Science Journal Classification (ASJC) codes

    • 化学 (全般)
    • 化学工学(全般)

    フィンガープリント

    「Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes」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