Comparison of Hydrogenases from Clostridium butyricum and Thiocapsa roseopersicina: Hydrogenases of C. butyricum and T.roseopersicina
The properties related to the temperature andoxygen stability of the cytoplasmic hydrogenases from thefermentative strict anaerobic bacterium, Clostridium butyricumNCIB 9576 (Cl. butyricum), and purple sulfur phototrophicbacterium, Thiocapsa roseopersicina NCIB 8347 (T.roseopersicina), were compared...
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Published in | Journal of microbiology and biotechnology pp. 1210 - 1215 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
한국미생물·생명공학회
01.08.2006
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Subjects | |
Online Access | Get full text |
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Summary: | The properties related to the temperature andoxygen stability of the cytoplasmic hydrogenases from thefermentative strict anaerobic bacterium, Clostridium butyricumNCIB 9576 (Cl. butyricum), and purple sulfur phototrophicbacterium, Thiocapsa roseopersicina NCIB 8347 (T.roseopersicina), were compared. The optimum temperaturesfor the growth of Cl. butyricum and T. roseopersicina were37oC and 25oC, respectively, whereas those for the H2 evolutionof the cytoplasmic hydrogenases prepared from Cl. butyricum(C-H2ase) and T. roseopersicina (T-H2ase) were 45oC and65oC, respectively. The T-H2ase was more thermostable thanthe C-H2ase and retained its ful activity for 5 h at 50oC underanaerobic conditions and 90% of its activity at 60oC, whereasthe C-H2ase lost its activity drastically at 50oC. The optimumpHs for H2 oxidation of the C-H2ase and T-H2ase were 9.02evolution activity at pH 7.0. Under aerobic conditions, 80%of the T-H2ase activity was retained for 10 h at 30oC, and50% of the activity remained after 6 days under the sameexperimental conditions. However, the C-H2ase was labile tooxygen and lost its activity immediately on exposure to air.Therefore, these properties of the T-H2ase are expected to beadvantageous for application in in vitro biological H2 productionsystems. KCI Citation Count: 9 |
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Bibliography: | G704-000169.2006.16.8.018 |
ISSN: | 1017-7825 |