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Synthesis and reactivity of β-cyclodextrin-histamine as enzyme model

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Abstract

Cyclodextrin (CD) has a hydrophobic cavity which acts like a binding site of an actual enzyme. But enzymatic turnover reaction did not occur in CD-catalyzed reactions. β-CD was modified by a histamine group to attach a reactive functional group. β-CD-histamine accelerates the hydrolysis of p-nitrophenyl acetate. Catalytic rate constant of this reaction is close to an actual enzyme, α-chymotrypsin. Enzymatic turnover reaction is realized with this compound at around neutral pH value.

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Authors and Affiliations

  1. Department of Chemical Engineering, Faculty of Engineering, Tokyo Institute of Technology, O-okayama, 152, Meguro-ku, Tokyo, Japan

    Tsukasa Ikeda, Ryoichi Kojin, Chul-joong Yoon, Hiroshi Ikeda, Masao Iijima, Kenjiro Hattori & Fujio Toda

Authors
  1. Tsukasa Ikeda
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  2. Ryoichi Kojin
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  3. Chul-joong Yoon
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  4. Hiroshi Ikeda
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  5. Masao Iijima
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  6. Kenjiro Hattori
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  7. Fujio Toda
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Ikeda, T., Kojin, R., Yoon, Cj. et al. Synthesis and reactivity of β-cyclodextrin-histamine as enzyme model. Journal of Inclusion Phenomena 2, 669–674 (1984). https://doi.org/10.1007/BF00662234

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  • DOI: https://doi.org/10.1007/BF00662234

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