Biomass conversion to fuels and chemicals

Patent metadata

Field	Value
Publication number	US-10017792-B2
Application number	US-201514804161-A
Country	US
Kind code	B2
Filing date	Jul 20, 2015
Priority date	Jul 18, 2014
Publication date	Jul 10, 2018
Grant date	Jul 10, 2018

Abstract

This disclosure relates to compositions and methods for converting biomass to various chemical intermediates and final products including fuels. Aspects include the depolymerization of lignin, cellulose, and hemicellulose to a wide slate of depolymerization compounds that can be subsequently metabolized by genetically modified bacterium, and converted to cis,cis-muconic acid. Other aspects include the use of monometallic catalysts for converting the cis,cis-muconic acid to commodity chemicals and fuels, for example adipic acid and/or nylon.

First claim

What is claimed is:

1. A genetically modified prokaryotic microorganism comprising:
an exogenous genetic addition encoding at least a 3-dehydroshikimate dehydratase and a phenol monoxygenase, wherein said genetically modified prokaryotic microorganism is capable of producing cis, cis-muconic acid.

2. The genetically modified prokaryotic microorganism of claim 1 , further comprising:
an endogenous gene deletion that ablates expression of at least one of a protocatechuic acid dioxygenase, a muconate lactonizing enzyme, or a muconolactone isomerase.

3. The genetically modified prokaryotic microorganism of claim 1 , further comprising:
an exogenous genetic addition encoding a vanillic acid demethylase.

4. The genetically modified prokaryotic microorganism of claim 1 , further comprising a deletion of an endogenous catabolite repression control gene.

5. The genetically modified prokaryotic microorganism of claim 1 , further comprising an exogenous genetic addition encoding at least a protocatechuic acid decarboxylase.

6. The genetically modified prokaryotic microorganism of claim 5 , wherein said protocatechuic acid decarboxylase comprises at least one of EcdB or EcdD.

7. The genetically modified prokaryotic microorganism of claim 1 , wherein said 3-dehydroshikimate dehydratase is from Bacillus cereus.

8. The genetically modified prokaryotic microorganism of claim 7 , wherein said 3-dehydroshikimate dehydratase comprises at least one of AroZ or AsbF.

9. The genetically modified prokaryotic microorganism of claim 1 , wherein said phenol monooxygenase is from Pseudomonas sp. CF600.

10. The genetically modified prokaryotic microorganism of claim 9 , wherein said phenol monooxygenase comprises at least one DmpKLMNOP or PheA.

11. The genetically modified prokaryotic microorganism of claim 2 , wherein said protocatechuic acid dioxygenase comprises at least one of PcaH or PcaG.

12. The genetically modified prokaryotic microorganism of claim 2 , wherein at least one of said muconate lactonizing enzyme or said muconolactone isomerase comprises at least one of CatB or CatC.

13. The genetically modified prokaryotic microorganism of claim 3 , wherein said vanillic acid demethylase comprises at least one of VanA, VanB, or LigM.

14. The genetically modified prokaryotic microorganism of claim 1 , wherein the genetically modified prokaryotic microorganism is from the genus Pseudomonas.

15. The genetically modified prokaryotic microorganism of claim 14 , wherein the genetically modified prokaryotic microorganism is P. putida, P. fluorescens , or P. stutzeri.

16. The genetically modified prokaryotic microorganism of claim 15 , wherein said genetically modified prokaryotic microorganism is P. putida KT2440.

17. The genetically modified prokaryotic microorganism of claim 10 , wherein said DmpKLMNOP has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID Nos: 24, 26, 28, 30, 32, and 34.

18. The genetically modified prokaryotic microorganism of claim 10 , wherein said PheA has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 36.

19. The genetically modified prokaryotic microorganism of claim 13 , wherein said LigM has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 38.

20. The genetically modified prokaryotic microorganism of claim 11 , wherein said PcaH has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 10.

21. The genetically modified prokaryotic microorganism of claim 11 , wherein said PcaG has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 12.

22. The genetically modified prokaryotic microorganism of claim 12 , wherein said CatB has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 2.

23. The genetically modified prokaryotic microorganism of claim 12 , wherein said CatC has an amino acid sequence that is at least 90% identical to the amino acid sequence set forth in SEQ ID NO: 4.

24. A process comprising:
contacting a culture broth comprising a lignin depolymerization compound with a genetically modified prokaryotic microorganism comprising a first exogenous genetic addition encoding at least a 3-dehydroshikimate dehydratase and a phenol monooxygenase, wherein:
said genetically modified prokaryotic microorganism is capable of converting at least a portion of said lignin depolymerization compound to cis, cis-muconic acid.

25. The process of claim 24 , wherein said lignin depolymerization compound comprises at least one of p-coumaric acid, ferulic acid, benzoic acid, phenol, coniferyl alcohol, caffeic acid, vanillin, or 4-hydroxybenzoic acid.

26. The process of claim 24 , wherein:
said culture broth further comprises a polysaccharide depolymerization compound, and
said genetically modified prokaryotic microorganism is capable of converting at least a portion of said polysaccharide depolymerization compound to cis, cis-muconic acid.

27. The process of claim 24 , wherein said polysaccharide depolymerization compound comprises at least one of glucose, xylose, arabinose, mannose, galactose, or rhamnose.

Assignees

• Alliance Sustainable Energy

Inventors

• Beckham Gregg T
• Johnson Christopher W
• Vardon Derek R
• Franden Mary Ann

Classifications

• C12Y113/11001

  Catechol 1,2-dioxygenase (1.13.11.1) · CPC title

• C07C51/47

  by solid-liquid treatment; by chemisorption · CPC title

• C12P7/44 Primary

  Polycarboxylic acids · CPC title

• C12Y402/01118

  3-Dehydroshikimate dehydratase (4.2.1.118) · CPC title

• C12N9/88

  Lyases (4.) · CPC title