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Covalent linking of alkaline protease on trichlorotriazine activated nylon

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Abstract

Alkaline protease was covalently attached to nylon using trichlorotriazine. Enzymatic activity was determined at different trichlorotriazine activation temperature and time. It was observed that, the optimum temperature and pH of the immobilized alkaline protease was comparable to that of the free enzyme. Immobilization improved the thermal stability and pH stability of the enzyme.

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Authors and Affiliations

  1. Department of Chemical Engineering, Anna University, 600 025, Madras, India

    M. Chellapandian

  2. Institute of Advanced Studies, University of Malaya, 59100, Kualalumpur, Malaysia

    C. A. Sastry

Authors
  1. M. Chellapandian
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  2. C. A. Sastry
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Chellapandian, M., Sastry, C.A. Covalent linking of alkaline protease on trichlorotriazine activated nylon. Bioprocess Engineering 15, 95–98 (1996). https://doi.org/10.1007/BF00372983

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  • DOI: https://doi.org/10.1007/BF00372983

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