• Title, Summary, Keyword: Clostridium thermoaceticum

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Production of Acetic Acid from Cellulosic Biomass (섬유성 바이오매스를 이용한 Acetic Acid 생산)

  • 우창호;박준호;윤현희
    • KSBB Journal
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    • v.15 no.5
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    • pp.458-463
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    • 2000
  • Production of acetic acid from cellulosic biomass by Simultaneous Saccharification and Extractive Fermentation (SSEF) was investigated. The homoacetate organism used in this study was a strain of Clostridium thermoaceticum, ATCC # 49707. A batch operation of Simultaneous Saccharification and Fermentation(SSF) using ${\alpha}$-cellulose at pH 5.5 and 55$^{\circ}C$ yielded 40% conversion of cellulose to acetic acid, while a fed-batch SSF operation produced a maximum acetic acid concentration of 25 g/L, with 50% overall yield. In-situ extractive fermentation to reduce the end-product inhibition on both bacteria and enzyme was carried out. in a batch SSEF using 200 g/L IRA-400 resin, acetic acid concentration reached to 23.9 g/L and acetic acid yield and productivity were observed to be 48% and 0.20 g/L-hr, respectively.

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EPR Studies of the Active Sites of Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum

  • Shin, Woonsup;Lindahl, Paul A.
    • Analytical Science and Technology
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    • v.8 no.4
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    • pp.869-876
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    • 1995
  • The active sites of the nickel and iron-containing enzyme, carbon monoxide dehydrogenase (CODH) from clostridium thermoaceticum were investigated using Electron Paramagnetic Resonance (EPR) technique. CODH exhibits several spectral features called NiFeC, $g_{ave}=1.82$, $g_{ave}=1.86$. FCII signals which are originated from different clusters in this enzyme. CODH is know to catalyze two different kinds of reactions - acetyl-CoA synthesis and CO oxidation. The acetyl-CoA synthesis activity can be followed by monitoring CO/acetyl-CoA exchange. The addition of 1,10-phenanthroline (phen) to CODH selectively destroyed the CO/acetyl-CoA exchange activity and eliminated the NiFeC signal completely. CO oxidation activity and other EPR signals were unaffected. Such behavior demonstrates that CODH has two distinct active sites and that the NiFe complex is only responsible for the CO/acctyl-CoA exchange activity. Phen caused the removal of only 30% of Ni in the NiFe complex ($0.3Ni/{\alpha}{\beta}$) as shown by the quantitative metal analysis. The phen-treated CODH could be reactivated fully by incubation In $Ni^{2+}$ solution. Radioactive $^{63}Ni^{2+}$ was used to quantitate the amount of the $Ni^{2+}$ incorporated into phen-treated enzyme and showed that the amount was the same as the removed by the phen treatment. i.e. $0.3Ni/{\alpha}{\beta}$. This indicates that only 30% of NiFe complexes are labile and responsible for the CO/acctyl-CoA exchange activity, the other 70% are non-labile and have no exchange activity. This is the first clear evidence that the NiFe complex is heterogencous and labile and non-labile Ni sites arc interacting differently with substrates and chelating agents like phen.

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Effect of Electrode Materials and Applied Potential in Electrocatalytic Reduction of Carbon Dioxide by Carbon Monoxide Dehydrogenase (일산화탄소탈수소화효소를 이용한 이산화탄소의 전기화학적 환원에 미치는 전극재료와 전위의 영향)

  • Shin, Jun Won;Kim, You-Sung;Song, Ji-Eun;Lee, Sang-Hee;Lee, Sang-Phil;Lee, Ho-Jun;Lim, Mi-Ran;Shin, Woon-Sup
    • Journal of the Korean Electrochemical Society
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    • v.11 no.3
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    • pp.165-169
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    • 2008
  • The effect of reduction of carbon dioxide by CODH(Carbon Monoxide Dehydrogenase) was compared on glassy carbon and gold working electrodes. In case of gold electrode, the choice of the optimum applied potential is very important since $H_2$ evolution can be mixed with $CO_2$ reduction. On the other hand, efficient $CO_2$ reduction was observed up to -650 mV vs. NHE on glassy carbon in neutral solution due to the larger overpotential for $H_2$ evolution on glassy carbon surface than that on gold surface. The optimum potential for $CO_2$ reduction was found to be $-570{\sim}600\;mV$ vs. NHE. The current efficiency of $CO_2$ to CO decreased dramatically at more negative potential according to the activity of enzyme decrease and the hydrogen evolution.