2018
DOI: 10.1016/j.ymben.2018.03.003
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From lignin to nylon: Cascaded chemical and biochemical conversion using metabolically engineered Pseudomonas putida

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Cited by 237 publications
(190 citation statements)
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“…At a titer of 62.5 g/L MA, the fermentation step in terms of environmental impact and variable costs was optimized for Scenarios C–F. This was the maximum concentration achieved in a laboratory‐scale bioreactor experiment with P. putida by Kohlstedt et al (2018) with catechol as the substrate. The same feeding strategy for glucose as C substrate applies for these simulations.…”
Section: Resultsmentioning
confidence: 99%
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“…At a titer of 62.5 g/L MA, the fermentation step in terms of environmental impact and variable costs was optimized for Scenarios C–F. This was the maximum concentration achieved in a laboratory‐scale bioreactor experiment with P. putida by Kohlstedt et al (2018) with catechol as the substrate. The same feeding strategy for glucose as C substrate applies for these simulations.…”
Section: Resultsmentioning
confidence: 99%
“…To optimize the conditions in the combination of a rectification step further research is required. In addition, metabolic engineering of P. putida KT2440‐BN6 is necessary to convert phenol and cresols besides catechol into MA, as shown by Nikel et al (2014), Vardon et al (2015), Shingler and Moore (1994), Guzik, Hupert‐Kocurek, Sitnik, and Wojcieszyńska, (2013), Kalil, Asyigin, and Zaki (2002), and Kohlstedt et al (2018). The ability to metabolically convert guaiacol by P. putida needs to be defined, because it was described for Amycolatopsis sp.…”
Section: Resultsmentioning
confidence: 99%
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“…The toxicity of catechol greatly limits its application as feedstock for bioconversion. With hydrothermal depolymerization of softwood lignin to catechol, phenol, and cresols, this strain accumulated muconic acid of 13 g/L and the small amount of 3-methyl muconic acid 142. A powerful promoter, P cat , was screened from diverse synthetic promoters by coupling with catA gene (encoding catechol 1,2-dioxygenases), which achieved overexpression of native catA and catA2.…”
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confidence: 99%