WO2009006662A4

WO2009006662A4 - Process for the oxidative cleavage of vinylaromatics using peroxidases or laccases

Info

Publication number: WO2009006662A4
Application number: PCT/AT2008/000250
Authority: WO
Inventors: Wolfgang Kroutil; Miguel Lara
Original assignee: Univ Graz; Wolfgang Kroutil; Miguel Lara
Priority date: 2007-07-10
Filing date: 2008-07-09
Publication date: 2009-06-04
Also published as: WO2009006662A2; WO2009006662A3

Abstract

The invention relates to a process for the oxidative cleavage of vinylaromatics of the formula (1), characterized in that compounds of the formula (1) are oxidized in the presence of molecular oxygen using at least one enzyme selected from among peroxidases and laccases as catalysts according to the reaction scheme below to form aldehydes or ketones of the formulae (2) and (3); where n is an integer from 0 to 5; the radicals R1 are selected from among saturated or unsaturated hydrocarbon groups which have from 1 to 10 carbon atoms and in which carbon atoms may be replaced by heteroatoms and may be further substituted, amino, C1-6-alkylamino and C1-6-dialkylamino groups, halogens, hydroxy and cyano, where two of the substituents R1 may be joined to form a ring; R2 and R3 are each, independently of one another, hydrogen or one of the options for R1, where R2 and/or R3 may be joined to an R1 to form a ring and R2 or R3 may each be a chemical bond.

Claims

AMENDED CLAIMS received by the International Bureau on 23 April 2009 (23.04.09)

1. A process for the oxidative cleavage of optionally substituted Vinylaro- mateπ the following formula (1) using at least one metalloprotein as a catalyst, characterized in that one or more compounds of formula (1) in the presence of molecular oxygen with at least one from Peroxidaseπ and Laccases selected enzyme is oxidized as a catalyst according to the general scheme below general reactants to aldehydes or ketones of the formulas (2) and (3):

wherein n is an integer from 0 to 5 such that the aromatic ring in ortho, meta and / or para position to the vinyl group may be substituted with 0 to 5 substituents R ¹ , which may be the same or different and are selected of: a) saturated or unsaturated Kohlenwasserstoffgruppeπ having 1 to 10 carbon atoms in which optionally one or more carbon atoms are replaced by a heteroatom selected from oxygen, nitrogen and sulfur, and optionally substituted with one or more substituents selected from Ci- ₆ - Alkyl groups, Cni-alkylene groups, Ci-β-alkoxy groups, amino, Ci-β-alkylamino and C ₁ . _6- dialkylamino groups, halogens, hydroxy, oxo and Cyaπo further substituted, b) amino, (^ ^ e-alkylamino and de-dialkylamino groups, and c) halogens, hydroxy and Cyaπo, wherein any two of the substituents R ¹ to an alicyclic or aromatic

Ring and in which the substituents R ² and R ^{3 are} each independently hydrogen or one of the options described under a), b) and c), wherein R ² and / or R ³ each having a substituent R ¹ to a alicyclic

Ring may be connected, in which case R ² and R ^{3 are} each for a chemical see bond between the carbon atom of the vinyl group to which they are attached, and the substituentπ R ^{1 can} stand.

2. The method according to claim 1, characterized in that the at least one enzyme from fungal peroxidases and laccases, haloperoxidases, lignin peroxidases, horseradish peroxidase and bovine milk peroxidase is selected.

3. The method according to claim 2, characterized in that the at least one enzyme from fungal peroxidases of Coprinus dnereus, from laccases of Coriolus versicolor, Agaricus bisporus and Candida rυgosa, laccase of Rhυs vemi- eifera, chloroperoxidase of Caldariomyces fumago and bromoperoxidases, e.g. of Streptomyces aureofaciens or Corallina officinalis.

4. The method according to claim 2 or 3, characterized in that the at least one enzyme from horseradish peroxidase, from peroxidases of Coprinus cere- reus and laccases of Coriolus versicolor and Agaricus bisporus is selected.

5. The method according to any one of the preceding claims, characterized in that the oxidation is carried out in a buffer.

6. The method according to claim 5, characterized in that the buffer is selected from Bis-Tris buffer, acetate buffer, formate buffer and phosphate buffer.

7. The method according to any one of the preceding claims, characterized in that the pH of the reaction is adjusted to 2 to 7.

8. The method according to any one of the preceding claims, characterized in that the oxidation is carried out under OrÜberdruck.

9. The method according to claim 8, characterized in that the oxidation is carried out under an O ₂ overpressure of 1 to 6 bar.

10. The method according to any one of the preceding claims, characterized in that the oxidation is carried out under the action of light.

11. The method according to any one of the preceding claims, characterized in that the oxidation is carried out in the presence of an organic solvent or solvent mixture.

12. The method according to claim 11, characterized in that the solvent or solvent mixture is used in a proportion of 1 to 20 vol .-% of Reaktioπs- mixture.

13. The method according to claim 11 or 12, characterized in that the organic solvent

Dimethyl sulfoxide, toluene, acetone, dioxane, tetrahydrofuran, dimethylformamide and mixtures thereof.

14. The method according to any one of the preceding claims, characterized in that is prepared as aldehyde of the formula (2) vanillin.

15. Use of fuπgaleπ peroxydases and laccases, fuming halogen peroxide, bacterial haloperoxidases, lignin peroxidases, horseradish Peroxi- dene or bovine milk peroxidase for catalysis of the oxidative cleavage of conjugated to the aromatic ring ethylenic double bonds optionally substituted Vinylaromateπ of the formula (1) , as defined in claim 1, with molecular oxygen.

16. Use according to claim 15, characterized in that at least one of fungal peroxidases of Coprinus cinereus, laccases of Coriolus versicolor, Agaricus bisporus or Candida rugosa, laccases of Rhus vemicifera, chloroperoxidase of Caldariomyces fumago and bromoperoxidases, such as Streptomyces aureofaciens or Corallina officinalis, selected enzyme is used as a catalyst.

17. Use according to claim 15 or 16, characterized in that at least one of horseradish peroxidase, Perox ^y Dasen Coprinus dnereus or laccases of Coriolus versicolor or Agaricus bisporus is used as catalyst.