Purification and characterization of two functional forms of intracellular protease PfpI from the hyperthermophilic archaeon Pyrococcus furiosus

Article Abstract:

Purification of two functional forms of intracellular protease P. furiosus protease I (PfpI) from the cell extracts of hyperthermophilic archaeon Pyrococcus furiosus reveals special characteristics. The predominant purified form is PfpI-C1, which is a hexamer and accounts for 90% of the total activity. The minor purified form, PfpI-C2, is a trimeric. The composition of both the forms is similar to that of PfpI purified by heat treatment. The proteolytic and half-life activities, thermal stability, substrates, and temperature optimum ranges of the two forms are discussed.

Archaeabacteria, Archaea

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Purification and characterization of a proteosome from the hyperthermophilic archaeon Pyrococcus furiosus

Article Abstract:

A four-step purification procedure was utilized for the isolation and characterization of the 20S proteosome of the thermophilic archaeon, Pyrococcus furiosus. The 640-kDa proteosome has a narrow substrate specificity when assayed with synthetic peptide substrates and contains an alpha (25-kDa) and a beta (22-kDa) subunit. Furthermore, the alpha and beta subunits of the proteosome were similar to the corresponding subunits of proteosomes from Thermoplasma acidophilum.

Microbial enzymes

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Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases

Article Abstract:

Research has been conducted on Pyrococcus furiosus which grows on chitin. The authors report that chitin is a growth substrate for P. furiosus, and that the biochemical features of chitinase family have been determined for their recombinant forms.

United States, Science & research, Environmental aspects, Genetic aspects, Growth, Chitin, Microbial growth, Microbiology, Microbial populations, Company growth, Microbial ecology

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