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A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin

The symmetrical structure of curcumin includes two 4-hydroxy-3-methoxyphenyl substructures. Laccase catalyzed formation of a phenol radical, radical migration and oxygen insertion at the benzylic positions can result in the formation of vanillin. As vanillin itself is a preferred phenolic substrate...

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Autores principales: Esparan, Vida, Krings, Ulrich, Struch, Marlene, Berger, Ralf G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272579/
https://www.ncbi.nlm.nih.gov/pubmed/25875042
http://dx.doi.org/10.3390/molecules20046640
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author Esparan, Vida
Krings, Ulrich
Struch, Marlene
Berger, Ralf G.
author_facet Esparan, Vida
Krings, Ulrich
Struch, Marlene
Berger, Ralf G.
author_sort Esparan, Vida
collection PubMed
description The symmetrical structure of curcumin includes two 4-hydroxy-3-methoxyphenyl substructures. Laccase catalyzed formation of a phenol radical, radical migration and oxygen insertion at the benzylic positions can result in the formation of vanillin. As vanillin itself is a preferred phenolic substrate of laccases, the formation of vanillin oligomers and polymers is inevitable, once vanillin becomes liberated. To decelerate the oligomerization, one of the phenolic hydroxyl groups was protected via acetylation. Monoacetyl curcumin with an approximate molar yield of 49% was the major acetylation product, when a lipase from Candida antarctica (CAL) was used. In the second step, monoacetyl curcumin was incubated with purified laccases of various basidiomycete fungi in a biphasic system (diethyl ether/aqueous buffer). A laccase from Funalia trogii (LccFtr) resulted in a high conversion (46% molar yield of curcumin monoacetate) to vanillin acetate. The non-protected vanillin moiety reacted to a mixture of higher molecular products. In the third step, the protecting group was removed from vanillin acetate using a feruloyl esterase from Pleurotus eryngii (PeFaeA) (68% molar yield). Alignment of the amino acid sequences indicated that high potential laccases performed better in this mediator and cofactor-free reaction.
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spelling pubmed-62725792018-12-03 A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin Esparan, Vida Krings, Ulrich Struch, Marlene Berger, Ralf G. Molecules Article The symmetrical structure of curcumin includes two 4-hydroxy-3-methoxyphenyl substructures. Laccase catalyzed formation of a phenol radical, radical migration and oxygen insertion at the benzylic positions can result in the formation of vanillin. As vanillin itself is a preferred phenolic substrate of laccases, the formation of vanillin oligomers and polymers is inevitable, once vanillin becomes liberated. To decelerate the oligomerization, one of the phenolic hydroxyl groups was protected via acetylation. Monoacetyl curcumin with an approximate molar yield of 49% was the major acetylation product, when a lipase from Candida antarctica (CAL) was used. In the second step, monoacetyl curcumin was incubated with purified laccases of various basidiomycete fungi in a biphasic system (diethyl ether/aqueous buffer). A laccase from Funalia trogii (LccFtr) resulted in a high conversion (46% molar yield of curcumin monoacetate) to vanillin acetate. The non-protected vanillin moiety reacted to a mixture of higher molecular products. In the third step, the protecting group was removed from vanillin acetate using a feruloyl esterase from Pleurotus eryngii (PeFaeA) (68% molar yield). Alignment of the amino acid sequences indicated that high potential laccases performed better in this mediator and cofactor-free reaction. MDPI 2015-04-14 /pmc/articles/PMC6272579/ /pubmed/25875042 http://dx.doi.org/10.3390/molecules20046640 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Esparan, Vida
Krings, Ulrich
Struch, Marlene
Berger, Ralf G.
A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title_full A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title_fullStr A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title_full_unstemmed A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title_short A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin
title_sort three-enzyme-system to degrade curcumin to natural vanillin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272579/
https://www.ncbi.nlm.nih.gov/pubmed/25875042
http://dx.doi.org/10.3390/molecules20046640
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