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Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol
Resveratrol, an ingredient of traditional Chinese medicine, has beneficial effects on human health and huge potential for application in modern medicine. Polydatin is extracted from plants and then deglycosylated into resveratrol; enzymatic methods are preferred for this reaction. In this study, a β...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8911618/ https://www.ncbi.nlm.nih.gov/pubmed/35268615 http://dx.doi.org/10.3390/molecules27051514 |
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author | Zhou, Jie Liang, Meng Lin, Yu Pang, Hao Wei, Yutuo Huang, Ribo Du, Liqin |
author_facet | Zhou, Jie Liang, Meng Lin, Yu Pang, Hao Wei, Yutuo Huang, Ribo Du, Liqin |
author_sort | Zhou, Jie |
collection | PubMed |
description | Resveratrol, an ingredient of traditional Chinese medicine, has beneficial effects on human health and huge potential for application in modern medicine. Polydatin is extracted from plants and then deglycosylated into resveratrol; enzymatic methods are preferred for this reaction. In this study, a β-D-glucosidase from Sphingomonas showed high efficiency in transforming polydatin into resveratrol and was tolerant toward organic solvents. Applying this enzyme in a biphasic transformation system resulted in 95.3% conversion of 20% concentration crude polydatin to resveratrol in 4 h. We thus report a new method for high-efficiency, clean production of resveratrol. |
format | Online Article Text |
id | pubmed-8911618 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89116182022-03-11 Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol Zhou, Jie Liang, Meng Lin, Yu Pang, Hao Wei, Yutuo Huang, Ribo Du, Liqin Molecules Article Resveratrol, an ingredient of traditional Chinese medicine, has beneficial effects on human health and huge potential for application in modern medicine. Polydatin is extracted from plants and then deglycosylated into resveratrol; enzymatic methods are preferred for this reaction. In this study, a β-D-glucosidase from Sphingomonas showed high efficiency in transforming polydatin into resveratrol and was tolerant toward organic solvents. Applying this enzyme in a biphasic transformation system resulted in 95.3% conversion of 20% concentration crude polydatin to resveratrol in 4 h. We thus report a new method for high-efficiency, clean production of resveratrol. MDPI 2022-02-23 /pmc/articles/PMC8911618/ /pubmed/35268615 http://dx.doi.org/10.3390/molecules27051514 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhou, Jie Liang, Meng Lin, Yu Pang, Hao Wei, Yutuo Huang, Ribo Du, Liqin Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title | Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title_full | Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title_fullStr | Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title_full_unstemmed | Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title_short | Application of β-Glucosidase in a Biphasic System for the Efficient Conversion of Polydatin to Resveratrol |
title_sort | application of β-glucosidase in a biphasic system for the efficient conversion of polydatin to resveratrol |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8911618/ https://www.ncbi.nlm.nih.gov/pubmed/35268615 http://dx.doi.org/10.3390/molecules27051514 |
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