Surfactant-lactoperoxidase complex catalytically active in organic media

Shin Ya Okazaki, Youichi Uchimura, Masahiro Goto, Shintaro Furusaki

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)


    A surfactant-lactoperoxidase (LPO) complex catalytically active in organic solvents was developed by the emulsion coating method. The oxidation of 2,6-dimethoxyphenol (2,6-DMP) was conducted by the surfactant-LPO complex in organic media. The LPO complex efficiently catalyzed the oxidation of 2,6-DMP in various organic solvents, although lyophilized LPO did not display the catalytic activity at all. To optimize the preparation and reaction conditions for the surfactant-LPO complex, we examined the effects of pH value in the water pools of W/O emulsions, kinds of oxidants, and the nature of organic solvents on the oxidation reaction. Its optimum activity was obtained when the pH value of the aqueous enzyme solution was adjusted to ca. 8 at the preparation stage. The LPO complex exhibited the highest catalytic activity in chloroform when H2O2 was employed as the oxidant. Furthermore, the storage stability of the surfactant-LPO complex was far better than that of the surfactant-horseradish peroxidase complex. This high storage stability of the LPO complex will be a benefit for industrial usage of peroxidases. (C) 2000 Elsevier Science S.A.

    Original languageEnglish
    Pages (from-to)103-107
    Number of pages5
    JournalBiochemical Engineering Journal
    Issue number2
    Publication statusPublished - 2000

    All Science Journal Classification (ASJC) codes

    • Biotechnology
    • Environmental Engineering
    • Bioengineering
    • Biomedical Engineering


    Dive into the research topics of 'Surfactant-lactoperoxidase complex catalytically active in organic media'. Together they form a unique fingerprint.

    Cite this