首页|Purification and characterization of a hydrogenase from the marine green alga Tetraselmis subcordiformis
Purification and characterization of a hydrogenase from the marine green alga Tetraselmis subcordiformis
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NETL
NSTL
Elsevier
Soluble hydrogenase from a marine green alga, Tetraselmis subcordiformis, was purified to homogeneity and characterized under strict anaerobic conditions. After a 4 h dark, anaerobic adaptation period for the algal culture, the hydrogenase showed a maximum in vitro hydrogen production activity of 148nmol H_2/(μg Chl a × h). The enzyme was purified 362-fold by a three-step process, and using reduced methyl viologen as the electron donor its activity was 61.67 U/mg at 25 C The optimum temperature and pH value for hydrogen production were 55 ℃ and 7.5, respectively. The N-terminal amino acid sequence of this 46kDa hydrogenase was determined, and it showed no homology to any known hydrogenase sequence.
characterizationhydrogenasemarine green algapurificationtetraselmis subcordiformis
Marine Byproducts Engineering Croup, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China ,Graduate School of the Chinese Academy of Sciences, Beijing 100039. China
Marine Byproducts Engineering Croup, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
Department of Food Engineering, Dalian Fisheries University, Dalian 116023, China
NETL
NSTL
Elsevier
