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Physiological responses to stress conditions and barophilic behavior of the hyperthermophilic vent archaeon Pyrococcus abyssi

Article Abstract:

The physiology of the deep-sea hyperthermophilic, anaerobic vent archaeon Pyrococcus abyssi from the Fiji Basin at a depth of 2,000 m was investigated under various conditions. Incubation under in situ pressure (20 MPa) and at 40 MPa increased the maximal and minimal growth temperatures by 4 degrees C. In situ pressure improved survival at a lethal high temperature (106 to 112 degrees C) relative to that at low pressure (0.3 MPa). The whole-cell protein profile did not change in cultures grown under low or high pressure at optimal and minimal growth temperatures.

Author: Marteinsson, Viggo Thor, Prieur, Daniel, Gambacorta, Agata, Moulin, Pascale, Birrien, Jean-Louis, Vernet, Marc
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
Marine bacteria

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Minimal amino acid requirements of the hyperthermophilic archaeon Pyrococcus abyssi, isolated from deep-sea hydrothermal vents

Article Abstract:

Experimental studies using hyperthermophilic sulfur-metabolizing archaeon Pyrococcus abyssi GE5, isolated from deep-sea hydrothermal vents, reveal that growth of these species requires a minimum of nine amino acids and vitamins as the sole carbon and energy sources. Cell densities and the generation time in the minimal growth medium are measured.

Author: Watrin, Laurent, Martin-Jezequel, Veronique, Prieur, Daniel
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Analysis, Physiological aspects, Microbial growth, Amino acids

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Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi

Article Abstract:

Researchers describe an alkaline phosphatase isolated from the hyperthermophilic archaeon Pyrococcus abyssi. The enzyme has a similar active site and many of the same structural elements as the Escherichia coli alkaline phosphatase.

Author: Zappa, Sebastien, Rolland, Jean-Luc, Flament, Didier, Gueguen, Yannick, Boudrant, Joseph, Dietrich, Jacques
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Microbial enzymes, Phosphatases

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Subjects list: Research, Bacteria, Thermophilic, Thermophiles
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