Converting Carbon Dioxide to Butyrate with an Engineered Strain of Clostridium ljungdahlii
نویسندگان
چکیده
منابع مشابه
Formic Acid Formation by Clostridium ljungdahlii at Elevated Pressures of Carbon Dioxide and Hydrogen
Low productivities of bioprocesses using gaseous carbon and energy sources are usually caused by the low solubility of those gases (e.g., H2 and CO). It has been suggested that increasing the partial pressure of those gases will result in higher dissolved concentrations and should, therefore, be helpful to overcome this obstacle. Investigations of the late 1980s with mixtures of hydrogen and ca...
متن کاملMicrobial electrosynthesis of butyrate from carbon dioxide.
This work proves for the first time the bioelectrochemical production of butyrate from CO2 as a sole carbon source. The highest concentration of butyrate achieved was 20.2 mMC, with a maximum butyrate production rate of 1.82 mMC d(-1). The electrochemical characterisation demonstrated that the CO2 reduction to butyrate was hydrogen driven. Production of ethanol and butanol was also observed ope...
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In this research, metabolic fixation of CO2 by growing cells of C. acetobutylicum cultivated with electrochemical reducing power was tested on the basis of the metabolites production and genes expression. In cyclic voltammetry, electrochemical oxidation and reduction reaction of neutral red (NR) immobilized in intact cells of C. acetobutylicum was stationarily repeated like the soluble one in t...
متن کاملLactose-inducible system for metabolic engineering of Clostridium ljungdahlii.
The development of tools for genetic manipulation of Clostridium ljungdahlii has increased its attractiveness as a chassis for autotrophic production of organic commodities and biofuels from syngas and microbial electrosynthesis and established it as a model organism for the study of the basic physiology of acetogenesis. In an attempt to expand the genetic toolbox for C. ljungdahlii, the possib...
متن کاملButyrate kinase from Clostridium acetobutylicum.
Crude extracts of Clostridium acetobutylicum contain a butyrate kinase of high specific activity (5.2 mumol/min/mg of protein). The enzyme has been purified 77-fold in a six-step procedure to a specific activity of 402 mumol/min/mg of protein. The purified butyrate kinase showed a single band with a molecular weight of 85,000 on nondenaturing polyacrylamide gradient gel electrophoresis. Separat...
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ژورنال
عنوان ژورنال: mBio
سال: 2014
ISSN: 2161-2129,2150-7511
DOI: 10.1128/mbio.01636-14