Pilot-Scale Production of Fatty Acid Ethyl Esters by an Engineered
            <i>Escherichia coli</i>
            Strain Harboring the p(Microdiesel) Plasmid

Elbahloul, Yasser; Steinbüchel, Alexander

doi:10.1128/aem.00515-10

Cited by 60 publications

(50 citation statements)

References 49 publications

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“…Later, this process was scaled up by cultivating the E. coli strain in 20 liters mineral salts medium using glucose or low-price glycerol and sodium oleate. In this pilot-scale production, a cellular FAEE content of approximately 25% (of CDW) was obtained (69).…”

Section: Atfa From a Baylyi Adp1: A Bacterial Model Enzyme For We Anmentioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

151

141

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SUMMARY Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few functions. Acyl thioesters are transferred by acyltransferases or transacylases to a variety of different substrates or are polymerized to lipophilic storage compounds. Lipases represent another important enzyme class dealing with fatty acyl chains; however, they cannot be regarded as acyltransferases in the strict sense. This review provides a detailed survey of the wide spectrum of bacterial acyltransferases and compares different enzyme families in regard to their catalytic mechanisms. On the basis of their studied or assumed mechanisms, most of the acyl-transferring enzymes can be divided into two groups. The majority of enzymes discussed in this review employ a conserved acyltransferase motif with an invariant histidine residue, followed by an acidic amino acid residue, and their catalytic mechanism is characterized by a noncovalent transition state. In contrast to that, lipases rely on completely different mechanism which employs a catalytic triad and functions via the formation of covalent intermediates. This is, for example, similar to the mechanism which has been suggested for polyester synthases. Consequently, although the presented enzyme types neither share homology nor have a common three-dimensional structure, and although they deal with greatly varying molecule structures, this variety is not reflected in their mechanisms, all of which rely on a catalytically active histidine residue.

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Section: Atfa From a Baylyi Adp1: A Bacterial Model Enzyme For We Anmentioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

151

141

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“…Previously reported renewable diesel cell factories have been mainly developed in the model organism E. coli , by expressing WS from A. baylyi ADP1, a bifunctional enzyme functioning as WS and DGAT and encoded by the gene a tfA [8,16-18]. However, the activity of WS from A. baylyi ADP1 for short-chain alcohols and the ability to form biodiesel is poor, which is one of the major limitations for biodiesel production.…”

Section: Introductionmentioning

confidence: 99%

Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production

Shi

Valle-Rodríguez

Khoomrung

et al. 2012

Biotechnol Biofuels

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Background Wax ester synthases (WSs) can synthesize wax esters from alcohols and fatty acyl coenzyme A thioesters. The knowledge of the preferred substrates for each WS allows the use of yeast cells for the production of wax esters that are high-value materials and can be used in a variety of industrial applications. The products of WSs include fatty acid ethyl esters, which can be directly used as biodiesel. Results Here, heterologous WSs derived from five different organisms were successfully expressed and evaluated for their substrate preference in Saccharomyces cerevisiae . We investigated the potential of the different WSs for biodiesel (that is, fatty acid ethyl esters) production in S. cerevisiae . All investigated WSs, from Acinetobacter baylyi ADP1, Marinobacter hydrocarbonoclasticus DSM 8798, Rhodococcus opacus PD630, Mus musculus C57BL/6 and Psychrobacter arcticus 273-4, have different substrate specificities, but they can all lead to the formation of biodiesel. The best biodiesel producing strain was found to be the one expressing WS from M. hydrocarbonoclasticus DSM 8798 that resulted in a biodiesel titer of 6.3 mg/L. To further enhance biodiesel production, acetyl coenzyme A carboxylase was up-regulated, which resulted in a 30% increase in biodiesel production. Conclusions Five WSs from different species were functionally expressed and their substrate preference characterized in S. cerevisiae , thus constructing cell factories for the production of specific kinds of wax ester. WS from M. hydrocarbonoclasticus showed the highest preference for ethanol compared to the other WSs, and could permit the engineered S. cerevisiae to produce biodiesel.

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“…The obtained strain was able to carry out the aerobic ethanol fermentation from sugars, as well as the enzymatic transesterification of this alcohol with the fatty acids derived from the lipidic metabolism, yielding FAEE, referred to as 'microdiesel' by the authors (Kalscheuer et al, 2006). Recently, Elbahloul and Steinbüchel have used the aforementioned microdiesel producing E. coli at a pilot plant scale, using glycerol and sodium oleate as carbon and fatty acids sources respectively, with promising results (Elbahloul & Steinbüchel, 2010). Nevertheless, their conclusions for both studies indicate that there is still a long way to go to the industrial application of their findings, and that the technique needs to be modified to make the engineered strains adaptable to different lipids rich sources and to lignocellulosic raw materials.…”

Section: Whole Cell Catalystsmentioning

confidence: 99%