Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in <Emphasis Type="Italic">Escherichia coli</Emphasis> |
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Authors: | Jaoon YH Kim Byung Hoon Jo Hyung Joon Cha |
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Institution: | (1) Department of Chemical Engineering, Pohang University of Science and Technology, 790-784 Pohang, Korea;(2) School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, 790-784 Pohang, Korea |
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Abstract: | Background Hydrogenases catalyze reversible reaction between hydrogen (H2) and proton. Inactivation of hydrogenase by exposure to oxygen is a critical limitation in biohydrogen production since strict
anaerobic conditions are required. While FeFe]-hydrogenases are irreversibly inactivated by oxygen, it was known that NiFe]-hydrogenases
are generally more tolerant to oxygen. The physiological function of NiFe]-hydrogenase 1 is still ambiguous. We herein investigated
the H2 production potential of NiFe]-hydrogenase 1 of Escherichia coli in vivo and in vitro. The hya A and hya B genes corresponding to the small and large subunits of NiFe]-hydrogenase 1 core enzyme, respectively, were expressed in
BL21, an E. coli strain without H2 producing ability. |
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