conjugated linoleic acid isomer
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Molecules ◽  
2019 ◽  
Vol 24 (9) ◽  
pp. 1753 ◽  
Author(s):  
Xun Wang ◽  
Qianjun Xia ◽  
Fei Wang ◽  
Yu Zhang ◽  
Xun Li

A novel recombinant strain has been constructed for converting glycerol into a specific conjugated linoleic acid isomer (trans-10, cis-12 CLA) using Yarrowia lipolytica as host. The lipid accumulation pathway was modified for increasing lipid content. Overexpression of the diacylglycerol transferase (DGA1) gene improved the intracellular lipid yield by approximately 45% as compared to the original strain. The corresponding intracellular lipid yield of recombinant strain WXYL037 reached 52.2% of the cell dry weight. In combination with integration of Δ12 desaturase from Mortierella alpina (MA12D) and DGA1, the linoleic acid (LA) production content reached 0.88 g/L, which was 2-fold that of the original strain. Furthermore, with overexpressed DGA1, MA12D and Propionibacterium acnes isomerase (PAI), the titer of trans-10, cis-12 CLA in WXYL037 reached 110.6 mg/L after 72 h of shake flask culture, representing a 201.8% improvement when compared with that attained in the WXYL030 strain, which manifested overexpressed PAI. With optimal medium, the maximum CLA content and lipid yield of Y. lipolytica Po1g were 132.6 mg/L and 2.58 g/L, respectively. This is the first report of the production of trans-10, cis-12 CLA by the oleaginous yeast Y. lipolytica using glycerol as the sole carbon source through expression of DGA1 combined with MA12D and PAI.


2014 ◽  
Vol 34 (2) ◽  
pp. 180-183 ◽  
Author(s):  
Francesca Maria Cicognini ◽  
Filippo Rossi ◽  
Samantha Sigolo ◽  
Antonio Gallo ◽  
Aldo Prandini

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e80900 ◽  
Author(s):  
Paolo Bergamo ◽  
Ennio Cocca ◽  
Rosanna Palumbo ◽  
Marta Gogliettino ◽  
Mose Rossi ◽  
...  

2010 ◽  
Vol 112 (2) ◽  
pp. 188-194 ◽  
Author(s):  
Lyndsey J. E. Dance ◽  
Olena Doran ◽  
Kathy Hallett ◽  
Dirk Dannenberger ◽  
Gerd Nuernberg ◽  
...  

2009 ◽  
Vol 191 (20) ◽  
pp. 6320-6328 ◽  
Author(s):  
Youjun Feng ◽  
John E. Cronan

ABSTRACT Recently, Nie and coworkers (L. Nie, Y. Ren, A. Janakiraman, S. Smith, and H. Schulz, Biochemistry 47:9618-9626, 2008) reported a new Escherichia coli thioesterase encoded by the ybaW gene that cleaves the thioester bonds of inhibitory acyl-coenzyme A (CoA) by-products generated during β-oxidation of certain unsaturated fatty acids. These authors suggested that ybaW expression might be regulated by FadR, the repressor of the fad (fatty acid degradation) regulon. We report mapping of the ybaW promoter and show that ybaW transcription responded to FadR in vivo. Moreover, purified FadR bound to a DNA sequence similar to the canonical FadR binding site located upstream of the ybaW coding sequence and was released from the promoter upon the addition of long-chain acyl-CoA thioesters. We therefore propose the designation fadM in place of ybaW. Although FadR regulation of fadM expression had the pattern typical of fad regulon genes, its modulation by the cyclic AMP (cAMP) receptor protein-cAMP complex (CRP-cAMP) global regulator was the opposite of that normally observed. CRP-cAMP generally acts as an activator of fad gene expression, consistent with the low status of fatty acids as carbon sources. However, glucose growth stimulated fadM expression relative to acetate growth, as did inactivation of CRP-cAMP, indicating that the complex acts as a negative regulator of this gene. The stimulation of fadM expression seen upon deletion of the gene encoding adenylate cyclase (Δcya) was reversed by supplementation of the growth medium with cAMP. Nie and coworkers also reported that growth on a conjugated linoleic acid isomer yields much higher levels of FadM thioesterase activity than does growth on oleic acid. In contrast, we found that the conjugated linoleic acid isomer was only a weak inducer of fadM expression. Although the gene is not essential for growth, the high basal level of fadM expression under diverse growth conditions suggests that the encoded thioesterase has functions in addition to β-oxidation.


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