Resumen

NOLASCO, Héctor; KUSHNER, Donald J.  y  OCHOA, José-Luis. Purification and Properties of an Extracellular Halophilic Serine-Protease from Haloferax mediterranei. Rev. Soc. Quím. Méx [online]. 2002, vol.46, n.3, pp.202-211. ISSN 0583-7693.

Na⁺, K⁺, and Mg⁺² ions are essential for Haloferax mediterranei growth and extra-cellular protease production. Ammonium ions (> 2 % w/v) reduce enzyme production, whereas Ca⁺² ions (~10 mM) enhance it and, in addition, activate the enzyme. The extra-cellular enzyme purified by ultra-filtration and Hydrophobic Interaction Chromatography, consists of a single polypeptide chain of MW 26 500 Da, with optimum activity at 3 M NaCl and pH 8 within 45 to 50 °C. This enzyme belongs to the serine-protease class and could be useful in a variety of industrial applications.

Palabras llave : Haloferax mediterranei; extracellular; protease; serine-proteases.

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