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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ftmdpi:oai:mdpi.com:/1420-3049/20/4/6640/ 2023-08-20T04:01:23+02:00 A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin Vida Esparan Ulrich Krings Marlene Struch Ralf Berger agris 2015-04-14 application/pdf https://doi.org/10.3390/molecules20046640 EN eng Multidisciplinary Digital Publishing Institute Natural Products Chemistry https://dx.doi.org/10.3390/molecules20046640 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 20; Issue 4; Pages: 6640-6653 vanillin curcumin lipase laccase esterase Text 2015 ftmdpi https://doi.org/10.3390/molecules20046640 2023-07-31T20:42:57Z 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. Text Antarc* Antarctica MDPI Open Access Publishing Molecules 20 4 6640 6653 |
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vanillin curcumin lipase laccase esterase |
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vanillin curcumin lipase laccase esterase Vida Esparan Ulrich Krings Marlene Struch Ralf Berger A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin |
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vanillin curcumin lipase laccase esterase |
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 |
Text |
author |
Vida Esparan Ulrich Krings Marlene Struch Ralf Berger |
author_facet |
Vida Esparan Ulrich Krings Marlene Struch Ralf Berger |
author_sort |
Vida Esparan |
title |
A Three-Enzyme-System to Degrade Curcumin to Natural Vanillin |
title_short |
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_sort |
three-enzyme-system to degrade curcumin to natural vanillin |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2015 |
url |
https://doi.org/10.3390/molecules20046640 |
op_coverage |
agris |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Molecules; Volume 20; Issue 4; Pages: 6640-6653 |
op_relation |
Natural Products Chemistry https://dx.doi.org/10.3390/molecules20046640 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/molecules20046640 |
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Molecules |
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20 |
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4 |
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6640 |
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6653 |
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1774724671729565696 |