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Prevention of limiting substrate diffusion in an immobilized enzyme reaction system: Lectin-induced activation of gel-entrapped β-D-galactosidase

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Summary

Escherichia coli β-D-galactosidase (EC 3.2.1.23) was entrapped in polyion complex-stabilized alginate gel beads together with a lectin fromRicinus communis (RCA1 lectin). The rate of entrapped enzyme-catalyzed hydrolysis of O-nitrophenyl-β-D-galactoside dramatically increased with an increase in lectin content, and at the maximum level of lection content the entrapped enzyme activity exceeded the native enzyme activity. A rapid decrease in the apparent Km was observed while increasing the lectin content, whereas the Vmax value varied insignificantly.

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Authors and Affiliations

  1. Institute of Applied Biochemistry, University of Tsukuba, Tsukuba-shi, Ibaraki 305, Japan

    Etsuo Kokufuta, Yoko Yamaya, Akihiko Shimada & Isei Nakamura

Authors
  1. Etsuo Kokufuta
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  2. Yoko Yamaya
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  3. Akihiko Shimada
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  4. Isei Nakamura
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Kokufuta, E., Yamaya, Y., Shimada, A. et al. Prevention of limiting substrate diffusion in an immobilized enzyme reaction system: Lectin-induced activation of gel-entrapped β-D-galactosidase. Biotechnol Lett 10, 301–306 (1988). https://doi.org/10.1007/BF01026155

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  • DOI: https://doi.org/10.1007/BF01026155

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