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Purification and characterization of the oxygen-thermostable hydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum camini

Paper ID Volume ID Publish Year Pages File Format Full-Text
21690 43235 2009 5 PDF Available
Title
Purification and characterization of the oxygen-thermostable hydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum camini
Abstract

Aeropyrum camini that was isolated from a deep-sea hydrothermal vent chimney, possessed two hydrogenases (161 and 85 kDa) in its soluble fraction. The 85-kDa hydrogenase was purified to homogeneity using several chromatography columns. The specific activities of the purified hydrogenase were: 14.8 μmol methyl viologenox/mg/min for hydrogen oxidation, and 14.6 μmol methyl viologenred/mg/min for proton reduction. The oxygen stabilities of hydrogenases that were purified from A. camini and the hydrogen thermophilic bacterium Persephonella hydrogeniphila, were compared. The hydrogenase purified from P. hydrogeniphila completely lost its activity following a 96-h exposure to atmosphere; however, the A. camini hydrogenase maintained 75% of its initial activity, even after a 168 h of atmospheric exposure. A. camini hydrogenase showed a half-life of 48 h at 90 °C, while P. hydrogeniphila hydrogenase showed complete denaturation after a 30 min incubation at the same temperature. Nine residues of the N-terminal amino acid sequence of A. camini hydrogenases (MARLLMIPGT) correspond to the protein sequence encoded by the hypothetical soluble hydrogenase subunit gene (APE2423) from A. pernix strain K1. A. camini hydrogenase has a high thermostability and is very tolerant to oxygen; therefore, it may be used for actual H2 production.

Keywords
Hydrogenase; Hyperthermophile; Crenarchaeota; Oxygen stability; Thermostability; H2 production
First Page Preview
Purification and characterization of the oxygen-thermostable hydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum camini
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 108, Issue 4, October 2009, Pages 299–303
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering