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 inJournal of microbiology and biotechnology pp. 1210 - 1215
Main Authors BAEK, JIN-SOOK, 최은혜, 윤영수, 김선창, 김미선
Format Journal Article
LanguageEnglish
Published 한국미생물·생명공학회 01.08.2006
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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
Bibliography:G704-000169.2006.16.8.018
ISSN:1017-7825