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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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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. |
format | Online Article Text |
id | pubmed-6272579 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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