IP Library Granted Patent US 10,113,188
Granted Patent B2
US 10,113,188 · App. 15/877,747 · Granted Oct 30, 2018

Compositions and methods for biological production of fatty acid derivatives

Inventor: Joshua A. Silverman (Los Altos Hills, CA)
Assignee: Calysta, Inc.
C12P7/6409C12N9/0006C12N9/0008C12N9/0026C12N9/0077C12N9/16C12N9/93C12N15/52C12P7/24C12P7/42C12P7/44C12P7/64C12P7/6436C12Y101/01C12Y101/01001C12Y102/99006C12Y301/02C12Y602/01
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Quick Facts
Patent No.
US 10,113,188
App. No.
15/877,747
Granted
Oct 30, 2018
Kind
B2
Abstract

The present disclosure provides compositions and methods for biologically producing fatty acid derivatives, such as fatty alcohols, from recombinant C 1 metabolizing microorganisms that utilize C 1 substrates such as methane or natural gas as a feedstock.

Claims (72)

1. A alpha-proteobacterial methanotroph, comprising a heterologous nucleic acid molecule encoding a fatty acid converting enzyme, wherein the alpha-proteobacterial methanotroph comprising the heterologous nucleic acid molecule encoding the fatty acid converting enzyme is capable of converting a C 1 substrate into a C 8 -C 24 fatty aldehyde, fatty alcohol, fatty ester wax, a hydroxy fatty acid, dicarboxylic acid, or a combination thereof, and wherein the encoded fatty acid converting enzyme comprises:

(a) a fatty acyl-CoA reductase capable of forming a fatty alcohol; or

(b) a fatty acyl-CoA reductase capable of forming a fatty aldehyde; or

(c) a carboxylic acid reductase; and

(d) a thioesterase; and/or

(e) an acyl-CoA synthetase.

2. The alpha-proteobacterial methanotroph according to claim 1 , wherein the host alpha-proteobacterial methanotroph is selected from Methylosinus trichosporium, Methylosinus sporium, Methylocystis parvus, Methylobacterium organophilum, Methylocella silvestris, Methylocella palustris, Methylocella tundrae, Methylocella daltona, Methylocystis bryophila, Methylocapsa aurea , or high growth variants thereof.

3. The alpha-proteobacterial methanotroph according to claim 1 , wherein the C 1 substrate is methane, natural gas, or unconventional natural gas.

4. The alpha-proteobacterial methanotroph according to claim 1 , wherein:

(a) the fatty acyl-CoA reductase capable of forming a fatty alcohol is FAR, CER4, or Maqu_2220; or

(b) the fatty acyl-CoA reductase capable of forming a fatty aldehyde is acr1.

5. The alpha-proteobacterial methanotroph according to claim 4 , wherein:

(a) the thioesterase is a tesA lacking a signal peptide, UcFatB or BTE; and/or

(b) the acyl-CoA synthetase is a FadD, yng1, or FAA2.

6. The alpha-proteobacterial methanotroph according to claim 5 , wherein:

(a) endogenous thioesterase activity is reduced, minimal or abolished as compared to unaltered endogenous thioesterase activity; and/or

(b) endogenous acyl-CoA synthetase activity is reduced, minimal or abolished as compared to unaltered endogenous acyl-CoA synthetase activity.

7. The alpha-proteobacterial methanotroph according to claim 5 , wherein the alpha-proteobacterial methanotroph further comprises a heterologous nucleic acid molecule encoding a P450 enzyme or monoxygenase enzyme to produce ω-hydroxy fatty acid.

8. The alpha-proteobacterial methanotroph according to claim 7 , wherein endogenous alcohol dehydrogenase activity is inhibited as compared to unaltered endogenous alcohol dehydrogenase activity.

9. The alpha-proteobacterial methanotroph according to claim 5 , wherein endogenous alcohol dehydrogenase activity is increased or elevated as compared to unaltered endogenous alcohol dehydrogenase activity to produce dicarboxylic acid.

10. The alpha-proteobacterial methanotroph according to claim 5 , wherein the alpha-proteobacterial methanotroph produces fatty alcohol comprising:

(a) one or more of C 8 -C 14 or C 10 -C 16 or C 14 -C 24 fatty alcohols;

(b) C 10 to C 18 fatty alcohol and the C 10 to C 18 fatty alcohols comprise at least 70% of the total fatty alcohol; or

(c) a branched chain fatty alcohol.

11. The alpha-proteobacterial methanotroph according to claim 1 , comprising:

(a) a heterologous nucleic acid molecule encoding an acyl-CoA independent fatty acyl-CoA reductase, and a heterologous nucleic acid molecule encoding a thioesterase, wherein the methanotroph is capable of converting a C 1 substrate into a C 8 -C 24 fatty alcohol;

(b) a heterologous nucleic acid molecule encoding an acyl-CoA dependent fatty acyl-CoA reductase, a heterologous nucleic acid molecule encoding a thioesterase, and a heterologous nucleic acid molecule encoding an acyl-CoA synthetase, wherein the methanotroph is capable of converting a C 1 substrate into a C 8 -C 24 fatty alcohol;

(c) a heterologous nucleic acid molecule encoding a carboxylic acid reductase, a heterologous nucleic acid molecule encoding a phosphopantetheinyl tranferase, and a heterologous nucleic acid molecule encoding an alcohol dehydrogenase, wherein the methanotroph is capable of converting a C 1 substrate into a C 8 -C 24 fatty alcohol;

(d) a heterologous nucleic acid molecule encoding a fatty acyl-CoA reductase, a heterologous nucleic acid molecule encoding a thioesterase, and a heterologous nucleic acid molecule encoding a P450 or monooxygenase, wherein the native alcohol dehydrogenase is inhibited, and wherein the methanotroph is capable of converting a C 1 substrate into a C 8 -C 24 ω-hydroxy fatty acid; or

(e) a heterologous nucleic acid molecule encoding a fatty acyl-CoA reductase, and a heterologous nucleic acid molecule encoding a thioesterase, wherein the methanotroph over-expresses native alcohol dehydrogenase as compared to the normal expression level of native alcohol dehydrogenase or comprises a heterologous nucleic acid molecule encoding an alcohol dehydrogenase or both, and wherein the methanotroph is capable of converting a C 1 substrate into a C 8 -C 24 dicarboxylic acid alcohol.

12. The alpha-proteobacterial methanotroph according to claim 11 , wherein the alpha-proteobacterial methanotroph is selected from Methylosinus trichosporium OB3b, Methylosinus sporium, Methylocystis parvus , or a high growth variant thereof.

13. A method for making a fatty acid derivative, comprising culturing a alpha-proteobacterial methanotroph with a C 1 substrate feedstock and recovering the fatty acid derivative,

wherein the alpha-proteobacterial methanotroph comprises a heterologous nucleic acid molecule encoding a fatty acid converting enzyme,

wherein the alpha-proteobacterial methanotroph converts the C 1 substrate into a C 8 -C 24 fatty acid derivative comprising a fatty aldehyde, a fatty alcohol, fatty ester wax, a hydroxy fatty acid, a dicarboxylic acid, or a combination thereof, and

wherein the encoded fatty acid converting enzyme comprises:

(a) a fatty acyl-CoA reductase capable of forming a fatty alcohol; or

(b) a fatty acyl-CoA reductase capable of forming a fatty aldehyde; or

(c) a carboxylic acid reductase; and

(d) a thioesterase; and/or

(e) an acyl-CoA synthetase.

14. The method according to claim 13 , wherein the alpha-proteobacterial methanotroph is selected from a Methylosinus trichosporium, Methylosinus sporium, Methylocystis parvus, Methylobacterium organophilum, Methylocella silvestris, Methylocella palustris, Methylocella tundrae, Methylocella daltona, Methylocystis bryophila, Methylocapsa aurea , or high growth variants thereof.

15. The method according to claim 13 , wherein the culture further comprises a heterologous bacterium.

16. The method according to claim 13 , wherein:

(a) the fatty acyl-CoA reductase capable of forming a fatty alcohol is FAR, CER4, or Maqu_2220; or

(b) the fatty acyl-CoA reductase capable of forming a fatty aldehyde is acr1.

17. The method according to claim 13 , wherein the thioesterase is a tesA lacking a signal peptide, UcFatB or BTE.

18. The method according to claim 17 , wherein endogenous thioesterase activity is reduced, minimal or abolished as compared to unaltered endogenous thioesterase activity.

19. The method according to claim 16 , wherein the acyl-CoA synthetase is FadD, yng1, or FAA2.

20. The method according to claim 16 , wherein endogenous acyl-CoA synthetase activity is reduced, minimal or abolished as compared to unaltered endogenous acyl-CoA synthetase activity.

21. The method according to claim 13 , further comprising a heterologous nucleic acid molecule encoding a P450 enzyme or monoxygenase enzyme to produce w-hydroxy fatty acid.

22. The method according to claim 21 , wherein endogenous alcohol dehydrogenase activity is reduced, minimal or abolished as compared to unaltered endogenous alcohol dehydrogenase activity.

23. The method according to claim 13 , wherein endogenous alcohol dehydrogenase activity is increased or elevated as compared to unaltered endogenous alcohol dehydrogenase activity to produce dicarboxylic acid.

24. The method according to claim 13 , wherein the alpha-proteobacterial methanotroph produces fatty alcohol comprising one or more of C 8 -C 14 or C 10 -C 16 or C 12 -C 14 or C 14 -C 18 or C 14 -C 24 fatty alcohols.

25. The method according to claim 13 , wherein the alpha-proteobacterial methanotroph produces fatty alcohol comprising C 10 to C 18 fatty alcohol and the C 10 to C 18 fatty alcohols comprise at least 70% of the total fatty alcohol.

26. The method according to claim 13 , wherein the alpha-proteobacterial methanotroph produces fatty alcohols comprising a branched chain fatty alcohol.

27. The method according to claim 13 , wherein the C 1 substrate is methane, natural gas, or unconventional natural gas.

28. The method according to claim 13 , wherein the C 1 substrate is methane, and the alpha-proteobacterial methanotrophs are cultured under aerobic conditions.

29. The method according to claim 13 , wherein the culturing is in a fermentor or bioreactor.

30. An aerobic, facultative methanotrophic bacteria, comprising a heterologous nucleic acid molecule encoding a fatty acid converting enzyme, wherein the facultative methanotrophic bacteria comprising the heterologous nucleic acid molecule encoding the fatty acid converting enzyme is capable of converting a C 1 substrate under aerobic conditions into a C 8 -C 24 fatty aldehyde, fatty alcohol, fatty ester wax, a hydroxy fatty acid, dicarboxylic acid, or a combination thereof, and wherein the encoded fatty acid converting enzyme comprises:

(a) a fatty acyl-CoA reductase capable of forming a fatty alcohol; or

(b) a fatty acyl-CoA reductase capable of forming a fatty aldehyde; or

(c) a carboxylic acid reductase; and

(d) a thioesterase; and/or

(e) an acyl-CoA synthetase.

31. The facultative methanotrophic bacteria according to claim 30 , wherein the host facultative methanotrophic bacteria is selected from Methylobacterium organophilum, Methylocella silvestris, Methylocella palustris, Methylocella tundrae, Methylocella daltona, Methylocystis bryophila, Methylocapsa aurea , or high growth variants thereof.

32. A methylotrophic bacteria, comprising a heterologous nucleic acid molecule encoding a fatty acid converting enzyme, wherein the methylotrophic bacteria comprising the heterologous nucleic acid molecule encoding the fatty acid converting enzyme is capable of converting a C 1 substrate under aerobic conditions into a C 8 -C 24 fatty aldehyde, fatty alcohol, fatty ester wax, a hydroxy fatty acid, dicarboxylic acid, or a combination thereof, and wherein the encoded fatty acid converting enzyme comprises:

(a) a fatty acyl-CoA reductase capable of forming a fatty alcohol; or

(b) a fatty acyl-CoA reductase capable of forming a fatty aldehyde; or

(c) a carboxylic acid reductase; and

(d) a thioesterase; and/or

(e) an acyl-CoA synthetase.

33. The methylotrophic bacteria according to claim 32 , wherein the host methylotrophic bacteria is selected from Methylobacterium extorquens, Methylobacterium radiotolerans, Methylobacterium populi, Methylobacterium chloromethanicum, Methylobacterium nodulans , or high growth variants thereof.

Assignments (2)
RELEASE OF SECURITY INTEREST Recorded Sep 12, 2025
From: VENTURE LENDING & LEASING IX, INC.
To: CALYSTA, INC.
Reel/Frame 072242/0047 →
SECURITY INTEREST Recorded Aug 27, 2021
From: CALYSTA, INC.
To: VENTURE LENDING & LEASING IX, INC.
Reel/Frame 057337/0355 →
Continuity (3)
Continuation 14441153
Provisional Application 61724733 · Nov 9, 2012
Related Publication 20180282769A1 · Oct 4, 2018