IP Library Granted Patent US 12,595,496
Granted Patent B2
US 12,595,496 · App. 17/420,908 · Granted Apr 7, 2026

Enzymatic biosynthesis of lactones

Inventors: Andreas W. Schirmer (Hayward, CA); Katherine Ann Murphy (San Diego, CA); Angelica Zabala Bautista (San Diego, CA)
Assignee: Genomatica, Inc.
C12P17/06C12N9/16C12N9/93C12Y301/0202C12Y602/01003
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 12,595,496
App. No.
17/420,908
Granted
Apr 7, 2026
Kind
B2
Abstract

The disclosure relates to methods for the production of natural lactones by bacteria under physiological conditions. The methods employ ybgC proteins having lactonizing activity.

Claims (23)

1 . A method for enzymatically producing a lactone under physiological conditions, the method comprising culturing a recombinant bacterium in the presence of a hydroxy acyl-CoA substrate, thereby producing said lactone, wherein said recombinant bacterium expresses a heterologous acyl-CoA thioesterase and a heterologous acyl-CoA synthetase protein, wherein:

the acyl-CoA thioesterase comprises a YbgC protein, wherein the YbgC protein has at least 85% amino acid sequence identity to any one of the amino acid sequence of SEQ ID NOs: 1-6, and wherein the YbgC protein converts a hydroxy acyl-CoA substrate to a lactone;

the hydroxy acyl-CoA substrate is a member selected from a 4-hydroxy acyl-CoA, a 5-hydroxy acyl-CoA, and a 6-hydroxy acyl-CoA; and

the YbgC protein converts the 4-hydroxy acyl-CoA to a γ-lactone, the YbgC protein converts the 5-hydroxy acyl-CoA to a δ-lactone, and the YbgC protein converts the 6-hydroxy acyl-CoA to a ε-lactone.

2 . The method of claim 1 , wherein the YbgC protein is overexpressed in said recombinant bacterium.

3 . The method of claim 1 , further comprising exogenously adding a fatty acid derivative molecule to the culture medium to produce said hydroxy acyl-CoA substrate from the recombinant bacterium.

4 . The method of claim 3 , wherein the fatty acid derivative molecule is a 4-hydroxy fatty acid derivative, a 5-hydroxy fatty acid derivative or a 6-hydroxy fatty acid derivative.

5 . The method of claim 4 , wherein the fatty acid derivative molecule is the 4-hydroxy fatty acid derivative and the recombinant bacterium produces 4-hydroxy acyl-CoA.

6 . The method of claim 5 , wherein the 4-hydroxy fatty acid derivative is 4-hydroxy decanoic acid, 4-hydroxy octanoic acid, 4-hydroxy dodecanoic acid, or 4-hydroxy tetranoic acid.

7 . The method of claim 4 , wherein the fatty acid derivative molecule is the 5-hydroxy fatty acid derivative and the recombinant bacterium produces 5-hydroxy acyl-CoA.

8 . The method of claim 7 , wherein the 5-hydroxy fatty acid derivative is 5-hydroxy decanoic acid.

9 . The method of claim 4 , wherein the fatty acid derivative molecule is the 6-hydroxy fatty acid derivative and the recombinant bacterium produces 6-hydroxy acyl-CoA.

10 . The method of claim 9 , wherein the 6-hydroxy fatty acid derivative is 6-hydroxy hexanoic acid or 6-hydroxy decanoic acid.

11 . The method of claim 1 , wherein the YbgC protein has at least 85% amino acid sequence identity to the amino acid sequence of SEQ ID NO: 1.

12 . The method of claim 1 , wherein the recombinant bacterium further expresses a second heterologous thioesterase and a heterologous hydroxylating enzyme.

13 . The method of claim 12 , wherein:

the second thioesterase is a member selected from the group consisting of the amino acid sequence of SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, and SEQ ID NO: 24; and

the hydroxylating enzyme is a member selected from the group consisting of the amino acid sequence of SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO; 29, SEQ ID NO: 30, and SEQ ID NO: 31.

14 . The method of claim 1 , wherein the recombinant bacterium produces the lactone from a simple carbon source.

15 . The method of claim 1 , wherein the recombinant bacterium comprises an endogenous acyl-CoA dehydrogenase that is attenuated or deleted or a 3-ketoacyl-CoA thiolase or dual 3-hydroxyacyl-CoA-dehydrogenase/dehydratase that is attenuated or deleted.

16 . The method of claim 1 , wherein the acyl-CoA synthetase is overexpressed.

17 . The method of claim 1 , further comprising recovering the lactone from the culture medium or isolating the lactone from the recombinant bacterium, or both.

18 . The method of claim 1 , wherein the lactone is produced without a chemical conversion step or acidification of the culture medium.

Assignments (4)
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 Jul 16, 2021
From: SCHIRMER, ANDREAS W.; MURPHY, KATHERINE ANN; BAUTISTA, ANGELICA ZABALA
To: GENOMATICA, INC.
Reel/Frame 056882/0718 →