Weibo Qiao’s research while affiliated with Beijing University of Chemical Technology and other places

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Publications (4)


Fig. 1 The designed sub-part of the 3-HP pathway in S. cerevisiae. The blue line indicates the glyoxylate cycle. Black font represents yeast endogenous enzymes, and yellow font represents exogenous enzymes. The dashed lines mean the conversion needs multi-step reactions. The blue color in chemical structures means the carbon atoms are from glyoxylate, and red color in chemical structures means the carbon atoms are from propionyl-CoA. ACC acetyl-CoA carboxylase, MCR malonyl-CoA reductase, HPCS 3-hydroxypropionyl-CoA synthase, PrpE propionyl-CoA synthetase, HPCD 3-hydroxypropionyl-CoA dehydratase, ACR acryloyl-CoA reductase, MCL malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase, MCH 2-methylfumaryl-CoA hydratase, ACH acetyl-CoA hydrolase, YciA acyl-CoA thioester hydrolase
Fig. 2 Construction of a 3-HP sub-pathway in S. cerevisiae. A Part of the 3-HP sub-pathway from propionate and glyoxylate. B GC-MS analysis of mesaconate produced from propionate and glyoxylate in engineered yeasts with various MCHs from different species. Strains were cultured with SC-dropout medium with 0.1% propionate and 0.1% glyoxylate. M01: CEN.PK 2-1D with the expression of SePrpE, RsMCL and EcYciA; M01-C: M01 with empty plasmid; M01-CaMCH: M01 with the expression of CaMCH; M01-RsMCH: M01 with the expression of RsMCH; M01-HmMCH: M01 with the expression of HmMCH. Mesaconate, the standard of mesaconate at 30 μg/L. C The yield of the reporter mesaconate from glucose. M201, strain M2 harboring the plasmid pSC-HIS-MCR for overexpressing MCR; M202, strain M2 harboring the plasmid pSC-HIS-MCR-YciA for overexpressing MCR and YciA. Strains were cultured with SC-dropout medium with 0.1% glyoxylate
Fig. 3 Functional validation of endogenous acyl-CoA hydrolases/transferases in yeast. A Production of mesaconate in yeast M3 with the overexpression of ACH1, EHD3 and TES1. M3-TRP: M3 harboring the empty plasmid pSC-TRP; M3-ACH1: M3 harboring the plasmid pSC-TRP-ACH1 for overexpressing ACH1; M3-EHD3: M3 harboring the plasmid pSC-TRP-EHD3 for overexpressing EHD3; M3-TES1: M3 harboring the plasmid pSC-TRP-TES1 for overexpressing TES1. B Production of mesaconate in yeast M3 with the knockout of ACH1, EHD3 and TES1; M3-ΔACH1: deletion of ACH1 in M3; M3-ΔEHD3: deletion of EHD3 in M3; M3-ΔTES1: deletion of TES1 in M3. Strains were cultured with SC-dropout medium with 0.1% propionate and 0.1% glyoxylate
Fig. 5 Optimization of the 3-HP sub-pathway in S. cerevisiae. A Evaluation of different 3-hydroxypropionyl-CoA synthases in the 3-HP sub-pathway. M101: strain M1 harboring the plasmid pSC-HIS-MsHPCS-MsACR -StHPCD and pUGG-PH for overexpressing MsHPCS, MsACR , StHPCD and MCR; M102: M1 harboring the plasmid pSC-HIS-SePrpE-MsACR -StHPCD and pUGG-PH for overexpressing SePrpE, MsACR , StHPCD and MCR; M103, M102 with an additional copy of SePrpE expression cassette in XII-1 site. B The yield of the reporter mesaconate from glucose. M201, strain M2 harboring the plasmid pSC-HIS-MCR for overexpressing MCR; M203, strain M2 harboring the plasmid pUGG-PH for overexpressing MCR; M403, the SePrpE expression cassette replaced the MsHPCS expression cassette at the XI-2 site of M203, and an additional copy of the SePrpE expression cassette was integrated into the XII-1 site; M405, strain M403 with additional copy of SePrpE in the plasmid pUGG-PH. Strains were cultured with SC-dropout medium with 0.1% glyoxylate
Exploiting a heterologous construction of the 3-hydroxypropionic acid carbon fixation pathway with mesaconate as an indicator in Saccharomyces cerevisiae
  • Article
  • Full-text available

May 2023

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169 Reads

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1 Citation

Bioresources and Bioprocessing

Shijie Xu

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Weibo Qiao

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Zuanwen Wang

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The 3-Hydroxypropionic acid (3-HP) pathway is one of the six known natural carbon fixation pathways, in which the carbon species used is bicarbonate. It has been considered to be the most suitable pathway for aerobic CO 2 fixation among the six natural carbon fixation pathways. Mesaconate is a high value-added derivative in the 3-HP pathway and can be used as a co-monomer to produce fire-retardant materials and hydrogels. In this study, we use mesaconate as a reporting compound to evaluate the construction and optimization of the sub-part of the 3-HP pathway in Saccharomyces cerevisiae . Combined with fine-tuning of the malonyl-CoA reductase (MCR-C and MCR-N) expression level and optimization of 3-Hydroxypropionyl-CoA synthase, the 3-HP sub-pathway was optimized using glucose or ethanol as the substrate, with the productions of mesaconate reaching 90.78 and 61.2 mg/L, respectively. Graphical Abstract

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Challenges and opportunities in C1-based biomanufacturing

October 2022

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99 Reads

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20 Citations

Bioresource Technology

The intensifying impact of green-house gas (GHG) emission on environment and climate change has attracted increasing attention, and biorefinery represents one of the most effective routes for reducing GHG emissions from human activities. However, this requires a shift for microbial fermentation from the current use of sugars to the use of biomass, and even better to the primary fixation of single carbon (C1) compounds. Here how microorganisms can be engineered for fixation and conversion of C1 compounds into metabolites that can serve as fuels and platform chemicals are reviewed. Meanwhile, key factors for utilization of these different pathways are discussed, followed by challenges and barriers for the development of C1-based biorefinery.


Engineering propionyl-CoA pools for de novo biosynthesis of odd-chain fatty acids in microbial cell factories

August 2022

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34 Reads

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10 Citations

Odd-chain fatty acids (OcFAs) and their derivatives have attracted great interest due to their wide applications in the food, pharmaceutical and petrochemical industries. Microorganisms can naturally de novo produce fatty acids (FAs), where mainly, even-chain with acetyl-CoA instead of odd-chain with propionyl-CoA is used as the primer. Usually, the absence of the precursor propionyl-CoA is considered the main reason that limits the efficient production of OcFAs. It is thus crucial to explore/evaluate/identify promising propionyl-CoA biosynthetic pathways to achieve large-scale biosynthesis of OcFAs. This review discusses the latest advances in microbial metabolism engineering toward producing propionyl-CoA and considers future research directions and challenges toward optimized production of OcFAs.

Citations (2)


... FALD is cheap and readily available, and plays an important role in the synthesis of many complex organic compounds that could be utilized as a starting material for the conversion of C1 molecules into multi-carbon high-value products. [7] GALD is commonly produced in industrial settings through the hydroformylation process of FALD by using rhodium or cobalt carbonyl catalysts, [8] and can also be produced from the condensation of two FALD molecules using biocatalyst such as C1 carboligases. [9] While controlling continuous carboligation reactions poses a challenge, glyoxylate carboligase (GCL) and glycolaldehyde synthase (GALS) have been reported to synthesize GALD through condensation of FALD. ...

Reference:

Enzymatic Production of Glycerol from Glycolaldehyde and Formaldehyde
Challenges and opportunities in C1-based biomanufacturing
  • Citing Article
  • October 2022

Bioresource Technology

... Microbial oils have also gained attention for their potential to produce nutraceutical fatty acids, like omega-3 and omega-6 polyunsaturated fatty acids (PUFAs), which can be used as fish oil substitutes [9]. Certain species, including the extensively studied yeast Y. lipolytica, the bacterium E. coli, and the marine heterotrophic microalga Schizochytrium sp., are prominent producers of odd-chain fatty acids (OCFAs), mostly C15:0, C17:0 and C17:1 [10,11]. These unusual fatty acids have recently attracted scientific interest due to their potential association with health benefits, despite being rare food components, mostly found in ruminant fat [12]. ...

Engineering propionyl-CoA pools for de novo biosynthesis of odd-chain fatty acids in microbial cell factories
  • Citing Article
  • August 2022