IP Library Granted Patent US 8,097,439
Granted Patent B2
US 8,097,439 · App. 12/575,427 · Granted Jan 17, 2012

Methods and compositions for producing fatty aldehydes

View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 8,097,439
App. No.
12/575,427
Granted
Jan 17, 2012
Kind
B2
Abstract

Methods and compositions, including nucleotide sequences, amino acid sequences, and host cells, for producing fatty aldehydes are described.

Claims (24)

1. A method of producing a fatty aldehyde, the method comprising:

(a) providing a bacterial host cell, said bacterial host cell engineered to express a gene encoding a polypeptide having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 22 (carB), and comprising the phosphopantetheine attachment site sequence of SEQ ID NO: 9, wherein the polypeptide has carboxylic acid reductase activity effective to convert a fatty acid to a fatty aldehyde; and

(b) culturing said engineered bacterial host cell in a culture media containing a carbohydrate carbon source under conditions effective to produce a fatty aldehyde at a yield of at least 25 mg/L in the media of the bacterial host cell culture, when cultured for 20 hours at 37° C.

2. The method of claim 1 , further comprising modifying the expression of a gene encoding a polypeptide having fatty acid synthase activity in the bacterial host cell.

3. The method of claim 2 , wherein said gene encodes a polypeptide having thioesterase activity.

4. The method of claim 1 , wherein the bacterial host cell is genetically engineered to express an attenuated level of a fatty acid degradation enzyme relative to a wild type bacterial host cell.

5. A method of producing a fatty aldehyde, the method comprising:

(a) providing a bacterial host cell, engineering said bacterial host cell engineered to comprise a recombinant vector comprising a nucleotide sequence having the nucleotide sequence of SEQ ID NO: 21, wherein the nucleotide sequence encodes a polypeptide having carboxylic acid reductase activity which comprises the phosphopantetheine attachment site sequence of SEQ ID NO: 9, and

(b) culturing said engineered bacterial host cell in a culture media containing a carbohydrate carbon source under conditions effective to produce a fatty aldehyde at a yield of at least 25 mg/L in the media of the bacterial host cell culture, when cultured for 20 hours at 37° C.

6. The method of claim 5 , further comprising modifying the expression of a gene encoding a polypeptide having fatty acid synthase activity in the bacterial host cell.

7. The method of claim 6 , wherein said gene encodes a polypeptide having thioesterase activity.

8. The method of claim 5 , wherein the bacterial host cell is a genetically engineered bacterial host cell that expresses an attenuated level of a fatty acid degradation enzyme relative to a wild type bacterial host cell, wherein the fatty acid degradation enzyme has acyl-CoA synthase (EC 2.3.1.86) activity.

9. The method of claim 1 , wherein the fatty aldehyde is isolated from the extracellular environment of the bacterial host cell.

10. The method of claim 1 , wherein the fatty aldehyde comprises a C 6 -C 26 fatty aldehyde.

11. The method of claim 10 , wherein the fatty aldehyde is decanal, dodecanal, myristal, or hexadecal.

12. The method of claim 1 , wherein the fatty aldehyde is an unsaturated fatty aldehyde.

13. The method of claim 1 , wherein the fatty aldehyde is a saturated fatty aldehyde.

14. The method of claim 1 , wherein said carbohydrate carbon source is a monosaccharide.

15. The method of claim 14 , wherein said monosaccharide is glucose.

16. The method of claim 15 , wherein the fatty aldehyde is extracted from the culture media.

17. The method of claim 1 , wherein the polypeptide comprises the reductase domain sequence of SEQ ID NO: 7, the NADP binding domain sequence of SEQ ID NO: 8 and the AMP binding domain sequence of SEQ ID NO: 10.

18. The method of claim 1 , wherein the polypeptide comprises an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 22.

19. The method of claim 1 , wherein the polypeptide comprises the amino acid sequence of SEQ ID NO: 22.

20. The method of claim 4 , wherein the fatty acid degradation enzyme has acyl-CoA synthase (EC 2.3.1.86) activity.

Assignments (7)
SECURITY INTEREST Recorded Feb 10, 2026
From: GENOMATICA, INC.
To: AGAIN BIO APS
Reel/Frame 074708/0001 →
SECURITY INTEREST Recorded Dec 9, 2025
From: GENOMATICA, INC.
To: NOVO HOLDINGS A/S, AS COLLATERAL AGENT
Reel/Frame 073915/0027 →
SECURITY INTEREST Recorded Jun 2, 2025
From: GENOMATICA, INC.
To: OXFORD FINANCE LLC
Reel/Frame 071471/0770 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 9, 2019
From: REG LIFE SCIENCES, LLC
To: GENOMATICA, INC.
Reel/Frame 050695/0661 →
CORRECTIVE ASSIGNMENT TO CORRECT THE SCHEDULE A, LINE 221 PREVIOUSLY RECORDED ON REEL 034193 FRAME 0175. ASSIGNOR(S) HEREBY CONFIRMS THE CORRECT APPLICATION NUMBER. Recorded Apr 7, 2015
From: LS9, INC.
To: REG LIFE SCIENCES, LLC
Reel/Frame 035391/0384 →
AMENDMENT TO PATENT ASSIGNMENT Recorded Nov 7, 2014
From: LS9, INC.
To: REG LIFE SCIENCES, LLC
Reel/Frame 034193/0175 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 22, 2009
From: ALIBHAI, MURTAZA F.; HU, ZHIHAO
To: LS9, INC.
Reel/Frame 023689/0396 →