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Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi
Provedor de dados: 5
Autores: Zappa, Sebastien; Rolland, Jean-luc; Flament, Didier; Gueguen, Yannick; Boudrant, Joseph; Dietrich, Jacques.
This work reports the first isolation and characterization of an alkaline phosphatase (AP) from a hyperthermophilic archaeon. An AP gene from Pyrococcus abyssi, a euryarchaeon isolated from a deep-sea hydrothermal vent, was cloned and the enzyme expressed in Escherichia coli. Analysis of the sequence showed conservation of the active site and structural elements of the E. coli AP. The recombinant AP was purified and characterized. Monomeric and homodimeric active forms were detected, with a monomer molecular mass of 54 kDa. Apparent optimum pH and temperature were estimated at 11.0 and 70 degreesC, respectively. Thus far, P. abyssi AP has been demonstrated to be the most thermostable AP, with half-lives at 100 and 105 degreesC of 18 and 5 h, respectively....
Tipo: Text
Palavras-chave: Escherichia coli; Characterization; Isolation; Gene; Alkaline phosphatase; Pyrococcus abyssi; Archaeon.
Ano: 2001
URL: http://archimer.ifremer.fr/doc/2001/publication-1268.pdf