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

Muneharu Goto, Chiaki Hatanaka, Kazuya Uezu, Masahiro Goto

    Research output: Contribution to journalArticlepeer-review

    1 Citation (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)565-567
    Number of pages3
    Journalkagaku kogaku ronbunshu
    Volume29
    Issue number4
    DOIs
    Publication statusPublished - Jul 2003

    All Science Journal Classification (ASJC) codes

    • Chemistry(all)
    • Chemical Engineering(all)

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