Comparison of hydrogenases from Clostridium butyricum and Thiocapsa roseopersicina: Hydrogenases of C-butyricum and T-roseopersicina

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The properties related to the temperature and oxygen stability of the cytoplasmic hydrogenases from the fermentative strict anaerobic bacterium, Clostridium butyricum NCIB 9576 (Cl. butyricum), and purple sulfur phototrophic bacterium, Thiocapsa roseopersicina NCIB 8347 (T. roseopersicina), were compared. The optimum temperatures for the growth of Cl. butyricum and T. roseopersicina were 37 degrees C and 25 degrees C, respectively, whereas those for the H, evolution of the cytoplasmic hydrogenases prepared from Cl. butyricum (C-H(2)ase) and T. roseopersicina (T-H(2)ase) were 45 degrees C and 65 degrees C, respectively. The T-H(2)ase was more thermostable than the C-H(2)ase and retained its full activity for 5 h at 50 degrees C under anaerobic conditions and 90% of its activity at 60 degrees C, whereas the C-H(2)ase lost its activity drastically at 50 degrees C. The optimum pHs for H-2 oxidation of the C-Hase and T-H(2)ase were 9.0 and 7.5, respectively. Both enzymes showed a maximum H-2 evolution activity at pH 7.0. Under aerobic conditions, 80% of the T-H(2)ase activity was retained for 10 h at 30 degrees C, and 50% of the activity remained after 6 days under the same experimental conditions. However, the C-H(2)ase was labile to oxygen and lost its activity immediately on exposure to air. Therefore, these properties of the T-(2)Hase are expected to be advantageous for application in in vitro biological H-2 production systems.
Publisher
KOREAN SOC MICROBIOLOGY BIOTECHNOLOGY
Issue Date
2006-08
Language
English
Article Type
Article
Keywords

CHLAMYDOMONAS-REINHARDTII UTEX-90; MEMBRANE-BOUND HYDROGENASE; NIFE HYDROGENASE; ACTIVATION

Citation

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.16, no.8, pp.1210 - 1215

ISSN
1017-7825
URI
http://hdl.handle.net/10203/90415
Appears in Collection
BS-Journal Papers(저널논문)
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