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1.
Chinese Journal of Biotechnology ; (12): 152-156, 2007.
Article in Chinese | WPRIM | ID: wpr-325402

ABSTRACT

Two hydrogen-producing bacterial strains were newly isolated and identified as Enterobacter sp. Z-16 and Clostridium sp. C-32 by 16S rDNA sequence analysis. Various parameters for hydrogen production, including substrates, initial pH and temperature, have been studied. The optimum condition for hydrogen production of strain Z-16 were achieved as: initial pH7.0, temperature 35 degrees C , sucrose as the favorite substrate. In comparison, The optimum condition for hydrogen production of strain C-32 were obtained as: initial pH8.0, temperature 35 degrees C , maltose as the favorite substrate . Under batch fermentative hydrogen production conditions, the maximal hydrogen conversion rate for strain Z-16 and strain C-32 were 2.68 mol H2/mol sucrose and 2.71mol H2/mol maltose, respectively. Using glucose as substrate, the hydrogen conversion rate of strain Z-16 and strain C-32 were 2.35 and 2.48 mol H2/mol glucose, respectively. This research suggest a good application potential of strain Z-16 and C-32 in the future biological hydrogen production.


Subject(s)
Clostridium , Metabolism , Enterobacter , Metabolism , Fermentation , Glucose , Metabolism , Hydrogen , Metabolism , Hydrogen-Ion Concentration , Maltose , Metabolism , Microscopy, Electron, Transmission , Polymerase Chain Reaction , RNA, Ribosomal, 16S , Genetics , Species Specificity , Sucrose , Metabolism , Temperature
2.
Chinese Journal of Biotechnology ; (12): 348-353, 2005.
Article in Chinese | WPRIM | ID: wpr-305271

ABSTRACT

Hydrogenases are enzymes that catalyse the oxidation of hydrogen and the reduction of protons. It plays an important role in the process of biohydrogen production. According to the metal atoms within hydrogenase, it can be classified as NiFe-hydrogenase, Fe-hydrogenase and metal-free hydrogenase. The overwhelming majority of hydrogenases are metalloenzymes. The metal atoms are involved in the forming of active site and [Fe-S] clusters. The active site directly catalyzes the reduction of protons and the oxidation of hydrogen. The [Fe-S] clusters are involved in the transport of electrons between the H2-activating site and the redox partners of hydrogenase. Presently, the crystal structures of NiFe-hydrogenase and Fe-hydrogenase from a few kinds of microorganism have been revealed. The metal-free hydrogenase, characterized by the absence of [Fe-S] cluster and the presence of an iron-containing cofactor, shows a great diversity comparing with those of NiFe-hydrogenases and Fe-hydrogenases. Recent progress have also indicated the mechanisms of activation.


Subject(s)
Catalysis , Catalytic Domain , Hydrogenase , Metabolism , Iron-Sulfur Proteins , Metabolism , Oxidation-Reduction
3.
Microbiology ; (12)1992.
Article in Chinese | WPRIM | ID: wpr-685537

ABSTRACT

Photosynthetic bacteria(PSB) showed great promise in biohydrogen production. Chromatium vinosum was able to utilize the fermentation waste of Klebsiella oxytoca for both photo-fermentative and dark-fermentative hydrogen production. The content of residual sugars and main organic acids decreased obviously after hydrogen production by C.vinosum. The maximal hydrogen production of C.vinosum was obtained at pH 6.5 adding extra 0.1%(W/W) NH_4Cl. Under photo-fermentative conditions, the content of butyric acid decreased by 54.38%, and the maximal hydrogen yield was 36.97 mL/mg cell. Under dark-fermentative conditions, the content of butyric acid decreased by 36.1% and the maximal hydrogen production was achieved as 37.50 mL/mg cell.

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