PUMA publications for /user/bastian/Butanols,https://puma.ub.uni-stuttgart.de/user/bastian/Butanols,PUMA RSS feed for /user/bastian/Butanols,2024-03-29T12:10:16+01:00Current knowledge on isobutanol production with Escherichia coli, Bacillus subtilis and Corynebacterium glutamicumhttps://puma.ub.uni-stuttgart.de/bibtex/20f88c2605071e1c350ed8a296eece367/bastianbastian2018-02-09T13:18:17+01:00Acids, Alcohol Bacillus Bacterial Butanols, Carboxy-Lyases, Corynebacterium Dehydrogenase, Engineering Escherichia Industrial Keto Metabolic Microbiology, Proteins, Recombinant coli, glutamicum, myown subtilis, <span data-person-type="author" class="authorEditorList "><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bastian Blombach" itemprop="url" href="/person/133960b6afe49761f6398812d65d1660e/author/0"><span itemprop="name">B. Blombach</span></a></span>, </span> and <span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bernhard J. Eikmanns" itemprop="url" href="/person/133960b6afe49761f6398812d65d1660e/author/1"><span itemprop="name">B. Eikmanns</span></a></span></span>. </span><span class="additional-entrytype-information"><span itemtype="http://schema.org/PublicationIssue" itemscope="itemscope" itemprop="isPartOf"><em><span itemprop="journal">Bioeng Bugs</span>, </em> <em><span itemtype="http://schema.org/PublicationVolume" itemscope="itemscope" itemprop="isPartOf"><span itemprop="volumeNumber">2 </span></span>(<span itemprop="issueNumber">6</span>):
<span itemprop="pagination">346--350</span></em> </span>(<em><span>December 2011<meta content="December 2011" itemprop="datePublished"/></span></em>)</span>Fri Feb 09 13:18:17 CET 2018Bioeng Bugsdec6346--350Current knowledge on isobutanol production with {Escherichia} coli, {Bacillus} subtilis and {Corynebacterium} glutamicum22011Acids, Alcohol Bacillus Bacterial Butanols, Carboxy-Lyases, Corynebacterium Dehydrogenase, Engineering Escherichia Industrial Keto Metabolic Microbiology, Proteins, Recombinant coli, glutamicum, myown subtilis, Due to steadily rising crude oil prices great efforts have been made to develop designer bugs for the fermentative production of higher alcohols, such as 2-methyl-1-butanol, 3-methyl-1-butanol and 2-Methyl-1-propanol (isobutanol), which all possess quality characteristics comparable to traditional oil based fuels. The common metabolic engineering approach uses the last two steps of the Ehrlich pathway, catalyzed by 2-ketoacid decarboxylase and an alcohol dehydrogenase converting the branched chain 2-ketoacids of L-isoleucine, L-leucine, and L-valine into the respective alcohols. This strategy was successfully used to engineer well suited and industrially employed bacteria, such as Escherichia coli, Bacillus subtilis and Corynebacterium glutamicum for the production of higher alcohols. Among these alcohols, isobutanol is currently the most promising one regarding final titer and yield. This article summarizes the current knowledge and achievements on isobutanol production with E. coli, B. subtilis and C. glutamicum regarding the metabolic engineering approaches and process conditions.The pyruvate dehydrogenase complex of Corynebacterium glutamicum: an attractive target for metabolic engineeringhttps://puma.ub.uni-stuttgart.de/bibtex/2ed56a8ffa25fcb7fe239b276b7e52493/bastianbastian2018-02-09T13:18:17+01:00Acid, Amino Butanols, Complex, Corynebacterium Dehydrogenase Engineering, Isobutanol Metabolic Pyruvate Pyruvic Valine, acid and complex dehydrogenase engineering, glutamicum, myown organic production, <span data-person-type="author" class="authorEditorList "><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bernhard J. Eikmanns" itemprop="url" href="/person/111bc42d6baae0b586acdbed655538eb6/author/0"><span itemprop="name">B. Eikmanns</span></a></span>, </span> and <span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bastian Blombach" itemprop="url" href="/person/111bc42d6baae0b586acdbed655538eb6/author/1"><span itemprop="name">B. Blombach</span></a></span></span>. </span><span class="additional-entrytype-information"><span itemtype="http://schema.org/PublicationIssue" itemscope="itemscope" itemprop="isPartOf"><em><span itemprop="journal">J. Biotechnol.</span>, </em> </span>(<em><span>December 2014<meta content="December 2014" itemprop="datePublished"/></span></em>)</span>Fri Feb 09 13:18:17 CET 2018J. Biotechnol.dec339--345The pyruvate dehydrogenase complex of {Corynebacterium} glutamicum: an attractive target for metabolic engineering192 Pt B2014Acid, Amino Butanols, Complex, Corynebacterium Dehydrogenase Engineering, Isobutanol Metabolic Pyruvate Pyruvic Valine, acid and complex dehydrogenase engineering, glutamicum, myown organic production, The pyruvate dehydrogenase complex (PDHC) catalyzes the oxidative thiamine pyrophosphate-dependent decarboxylation of pyruvate to acetyl-CoA and CO2. Since pyruvate is a key metabolite of the central metabolism and also the precursor for several relevant biotechnological products, metabolic engineering of this multienzyme complex is a promising strategy to improve microbial production processes. This review summarizes the current knowledge and achievements on metabolic engineering approaches to tailor the PDHC of Corynebacterium glutamicum for the bio-based production of l-valine, 2-ketosiovalerate, pyruvate, succinate and isobutanol and to improve l-lysine production.Corynebacterium glutamicum tailored for efficient isobutanol productionhttps://puma.ub.uni-stuttgart.de/bibtex/2a0a5fcfba6017eb6a61292baef557af7/bastianbastian2018-02-09T13:18:17+01:00Anaerobiosis, Bacterial Bacterial, Butanols, Chromosomes, Corynebacterium Escherichia Fungal Glucose, Lactococcus Metabolic Networks Pathways, Plasmids, Proteins Proteins, Recombinant Saccharomyces and cerevisiae, coli, glutamicum, lactis, myown <span data-person-type="author" class="authorEditorList "><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bastian Blombach" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/0"><span itemprop="name">B. Blombach</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Tanja Riester" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/1"><span itemprop="name">T. Riester</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Stefan Wieschalka" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/2"><span itemprop="name">S. Wieschalka</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Christian Ziert" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/3"><span itemprop="name">C. Ziert</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Jung-Won Youn" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/4"><span itemprop="name">J. Youn</span></a></span>, </span><span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Volker F. Wendisch" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/5"><span itemprop="name">V. Wendisch</span></a></span>, </span> and <span><span itemtype="http://schema.org/Person" itemscope="itemscope" itemprop="author"><a title="Bernhard J. Eikmanns" itemprop="url" href="/person/10ff226fcd2ff0614810a1890f8f46f8e/author/6"><span itemprop="name">B. Eikmanns</span></a></span></span>. </span><span class="additional-entrytype-information"><span itemtype="http://schema.org/PublicationIssue" itemscope="itemscope" itemprop="isPartOf"><em><span itemprop="journal">Appl. Environ. Microbiol.</span>, </em> <em><span itemtype="http://schema.org/PublicationVolume" itemscope="itemscope" itemprop="isPartOf"><span itemprop="volumeNumber">77 </span></span>(<span itemprop="issueNumber">10</span>):
<span itemprop="pagination">3300--3310</span></em> </span>(<em><span>May 2011<meta content="May 2011" itemprop="datePublished"/></span></em>)</span>Fri Feb 09 13:18:17 CET 2018Appl. Environ. Microbiol.may103300--3310Corynebacterium glutamicum tailored for efficient isobutanol production772011Anaerobiosis, Bacterial Bacterial, Butanols, Chromosomes, Corynebacterium Escherichia Fungal Glucose, Lactococcus Metabolic Networks Pathways, Plasmids, Proteins Proteins, Recombinant Saccharomyces and cerevisiae, coli, glutamicum, lactis, myown We recently engineered Corynebacterium glutamicum for aerobic production of 2-ketoisovalerate by inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone oxidoreductase, transaminase B, and additional overexpression of the ilvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase. Based on this strain, we engineered C. glutamicum for the production of isobutanol from glucose under oxygen deprivation conditions by inactivation of l-lactate and malate dehydrogenases, implementation of ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2 (ADH2) from Saccharomyces cerevisiae, and expression of the pntAB transhydrogenase genes from Escherichia coli. The resulting strain produced isobutanol with a substrate-specific yield (Y(P/S)) of 0.60 ± 0.02 mol per mol of glucose. Interestingly, a chromosomally encoded alcohol dehydrogenase rather than the plasmid-encoded ADH2 from S. cerevisiae was involved in isobutanol formation with C. glutamicum, and overexpression of the corresponding adhA gene increased the Y(P/S) to 0.77 ± 0.01 mol of isobutanol per mol of glucose. Inactivation of the malic enzyme significantly reduced the Y(P/S), indicating that the metabolic cycle consisting of pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase, and malic enzyme is responsible for the conversion of NADH + H+ to NADPH + H+. In fed-batch fermentations with an aerobic growth phase and an oxygen-depleted production phase, the most promising strain, C. glutamicum ΔaceE Δpqo ΔilvE ΔldhA Δmdh(pJC4ilvBNCD-pntAB)(pBB1kivd-adhA), produced about 175 mM isobutanol, with a volumetric productivity of 4.4 mM h⁻¹, and showed an overall Y(P/S) of about 0.48 mol per mol of glucose in the production phase.