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Partial purification and characterization of two proteases fromAgave fourcroydes

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Abstract

Large amounts of wastes are produced by the henequen industry from which it may be possible to obtain products of commercial importance. Our laboratory has detected proteolytic activity inAgave fourcroydes (henequen) juice. The proteolytic activity is a result of two proteases of 14,500 and 12,000 daltons, respectively. Both enzymes are very stable at -20°C., when freeze-dried and in the presence of EDTA and cysteine. They differ in pH optimum and thermal stability.

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Authors and Affiliations

  1. Division de Biologia Vegetal, Centro de Investigación Cientifica Yucatán, Apdo, Postal 87, CP 97310, Cordemex, Yucatán, México

    Miriam Monforte & Victor M. Loyola-Vargas

  2. Centro de Graduados e Investigation del Instituto Tecnológico de Mérida, sucursal D, Apdo Postal 136, CP 97100, Mérida, Yuc., México

    Miguel Cedeno

  3. Departamento de Bioquimica, Facultad de Quimica, UMAM., CP 04510, México D. F.

    Miguel Cedeno

Authors
  1. Miriam Monforte
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  2. Miguel Cedeno
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  3. Victor M. Loyola-Vargas
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Monforte, M., Cedeno, M. & Loyola-Vargas, V.M. Partial purification and characterization of two proteases fromAgave fourcroydes . Appl Biochem Biotechnol 15, 245–254 (1987). https://doi.org/10.1007/BF02798452

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  • DOI: https://doi.org/10.1007/BF02798452

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