IP Library › Granted Patent US 9,617,564
Granted Patent B2
US 9,617,564 · App. 14/607,328 · Granted Apr 11, 2017

Production of volatile dienes by enzymatic dehydration of light alkenols

Inventor: Philippe Marliere (Mouscron, BE)
Assignee: Scientist of Fortune, S.A.
C12P5/026C12N9/88C12P5/007C12Y402/01127
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Quick Facts
Patent No.
US 9,617,564
App. No.
14/607,328
Granted
Apr 11, 2017
Kind
B2
Abstract

Described is a method for generating conjugated dienes through a biological process. More specifically, the application describes a method for producing conjugated dienes (for example butadiene, isoprene or dimethylbutadiene) from light alkenols via enzymatic dehydration, in particular by making use of an alkenol dehydratase.

Claims (38)

1. A method for producing a conjugated diene comprising enzymatically converting a C n H 2n O into C n H 2n-2 +H 2 O, wherein 3<n<7, by an enzyme at least 70% identical to the amino acid sequence of SEQ ID NO:1 wherein said enzyme has alkenol dehydratase activity.

2. The method of claim 1 , wherein said method is carried out in vitro.

3. The method of claim 1 , wherein said method is carried out in a microorganism.

4. The method of claim 1 , wherein C n H 2n O is C 4 H 8 O.

5. The method of claim 4 , wherein the C 4 H 8 O is but-2-en-1-ol, but-3-en-2-ol, or but-3-en-1-ol.

6. The method of claim 5 , wherein 1,3-butadiene is recovered.

7. The method of claim 1 , wherein C n H 2n O is C 5 H 10 O.

8. The method of claim 7 , wherein the C 5 H 10 O is 3-methylbut-3-en-1-ol, 2-methylbut-2-en-1-ol, 3-methylbut-3-en-2-ol, or 2-methylbut-3-en-1-ol.

9. The method of claim 8 , wherein isoprene is recovered.

10. The method of claim 1 , wherein C n H 2n O is C 6 H 12 O.

11. The method of claim 10 , wherein the C 6 H 12 O is are 2,3-dimethylbut-2-en-1-ol, 2,3-dimethylbut-3-en-2-ol and 2,3-dimethylbut-3-en-1-ol.

12. The method of claim 11 , wherein dimethyl-butadiene is recovered.

13. The method of claim 10 , wherein the enzyme is at least 75% identical to the amino acid sequence of SEQ ID NO:1.

14. The method of claim 10 , wherein the enzyme is at least 80% identical to the amino acid sequence of SEQ ID NO:1.

15. The method of claim 10 , wherein the enzyme is at least 90% identical to the amino acid sequence of SEQ ID NO:1.

16. The method of claim 10 , wherein the enzyme is the amino acid sequence of SEQ ID NO:1.

17. A composition comprising a microorganism comprising an enzyme at least 70% identical to the amino acid sequence of SEQ ID NO:1, wherein said enzyme has alkenol dehydratase activity, and a C n H 2n O alcohol, wherein 3<n<7.

18. The composition of claim 17 , wherein C n H 2n O is C 4 H 8 O.

19. The composition of claim 18 , wherein the C 4 H 8 O is but-2-en-1-ol, but-3-en-2-ol, or but-3-en-1-ol.

20. The composition of claim 17 , wherein C n H 2n O is C 5 H 10 O.

21. The composition of claim 20 , wherein the C 5 H 10 O is 3-methylbut-3-en-1-ol, 2-methylbut-2-en-1-ol, 3-methylbut-3-en-2-ol, or 2-methylbut-3-en-1-ol.

22. The composition of claim 17 , wherein C n H 2n O is C 6 H 12 O.

23. The composition of claim 10 , wherein the C 6 H 12 O is are 2,3-dimethylbut-2-en-1-ol, 2,3-dimethylbut-3-en-2-ol and 2,3-dimethylbut-3-en-1-ol.

24. The composition of claim 22 , wherein the enzyme is at least 75% identical to the amino acid sequence of SEQ ID NO:1.

25. The composition of claim 22 , wherein the enzyme is at least 80% identical to the amino acid sequence of SEQ ID NO:1.

26. The composition of claim 22 , wherein the enzyme is at least 90% identical to the amino acid sequence of SEQ ID NO:1.

27. The composition of claim 22 , wherein the enzyme is the amino acid sequence of SEQ ID NO:1.

28. A composition comprising an enzyme at least 70% identical to the amino acid sequence of SEQ ID NO:1, wherein said enzyme has alkenol dehydratase activity, and a C n H 2n O alcohol, wherein 3<n<7.

29. The composition of claim 28 , wherein C n H 2n O is C 4 H 8 O.

30. The composition of claim 29 , wherein the C 4 H 8 O is but-2-en-1-ol, but-3-en-2-ol, or but-3-en-1-ol.

31. The composition of claim 28 , wherein C n H 2n O is C 5 H 10 O.

32. The composition of claim 31 , wherein the C 5 H 10 O is 3-methylbut-3-en-1-ol, 2-methylbut-2-en-1-ol, 3-methylbut-3-en-2-ol, or 2-methylbut-3-en-1-ol.

33. The composition of claim 28 , wherein C n H 2n O is C 6 H 12 O.

34. The composition of claim 33 , wherein the C 6 H 12 O is are 2,3-dimethylbut-2-en-1-ol, 2,3-dimethylbut-3-en-2-ol and 2,3-dimethylbut-3-en-1-ol.

35. The composition of claim 28 , wherein the enzyme is at least 75% identical to the amino acid sequence of SEQ ID NO:1.

36. The composition of claim 28 , wherein the enzyme is at least 80% identical to the amino acid sequence of SEQ ID NO:1.

37. The composition of claim 28 , wherein the enzyme is at least 90% identical to the amino acid sequence of SEQ ID NO:1.

38. The composition of claim 28 , wherein the enzyme is the amino acid sequence of SEQ ID NO:1.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded May 14, 2017
From: MARLIERE, PHILIPPE
To: SCIENTIST OF FORTUNE, S.A.
Reel/Frame 042369/0765 →
Priority Claims (1)
EP 12182270 · Aug 29, 2012 · regional
Continuity (3)
Continuation 14195738 · Mar 3, 2014
Continuation 13957482 · Aug 2, 2013
Related Publication 20150140631A1 · May 21, 2015