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Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis
Hyperoside (quercetin 3-O-galactoside) exhibits many biological functions, along with higher bioactivities than quercetin. In this study, three UDP-dependent glycosyltransferases (UGTs) were screened for efficient hyperoside synthesis from quercetin. The highest hyperoside production of 58.5 mg·L(−1...
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/PMC8949062/ https://www.ncbi.nlm.nih.gov/pubmed/35336203 http://dx.doi.org/10.3390/microorganisms10030628 |
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author | Li, Guosi Zhu, Fucheng Wei, Peipei Xue, Hailong Chen, Naidong Lu, Baowei Deng, Hui Chen, Cunwu Yin, Xinjian |
author_facet | Li, Guosi Zhu, Fucheng Wei, Peipei Xue, Hailong Chen, Naidong Lu, Baowei Deng, Hui Chen, Cunwu Yin, Xinjian |
author_sort | Li, Guosi |
collection | PubMed |
description | Hyperoside (quercetin 3-O-galactoside) exhibits many biological functions, along with higher bioactivities than quercetin. In this study, three UDP-dependent glycosyltransferases (UGTs) were screened for efficient hyperoside synthesis from quercetin. The highest hyperoside production of 58.5 mg·L(−1) was obtained in a recombinant Escherichia coli co-expressing UGT from Petunia hybrida (PhUGT) and UDP-glucose epimerase (GalE, a key enzyme catalyzing the conversion of UDP-glucose to UDP-galactose) from E. coli. When additional enzymes (phosphoglucomutase (Pgm) and UDP-glucose pyrophosphorylase (GalU)) were introduced into the recombinant E. coli, the increased flux toward UDP-glucose synthesis led to enhanced UDP-galactose-derived hyperoside synthesis. The efficiency of the recombinant strain was further improved by increasing the copy number of the PhUGT, which is a limiting step in the bioconversion. Through the optimization of the fermentation conditions, the production of hyperoside increased from 245.6 to 411.2 mg·L(−1). The production was also conducted using a substrate-fed batch fermentation, and the maximal hyperoside production was 831.6 mg·L(−1), with a molar conversion ratio of 90.2% and a specific productivity of 27.7 mg·L(−1)·h(−1) after 30 h of fermentation. The efficient hyperoside synthesis pathway described here can be used widely for the glycosylation of other flavonoids and bioactive substances. |
format | Online Article Text |
id | pubmed-8949062 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89490622022-03-26 Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis Li, Guosi Zhu, Fucheng Wei, Peipei Xue, Hailong Chen, Naidong Lu, Baowei Deng, Hui Chen, Cunwu Yin, Xinjian Microorganisms Article Hyperoside (quercetin 3-O-galactoside) exhibits many biological functions, along with higher bioactivities than quercetin. In this study, three UDP-dependent glycosyltransferases (UGTs) were screened for efficient hyperoside synthesis from quercetin. The highest hyperoside production of 58.5 mg·L(−1) was obtained in a recombinant Escherichia coli co-expressing UGT from Petunia hybrida (PhUGT) and UDP-glucose epimerase (GalE, a key enzyme catalyzing the conversion of UDP-glucose to UDP-galactose) from E. coli. When additional enzymes (phosphoglucomutase (Pgm) and UDP-glucose pyrophosphorylase (GalU)) were introduced into the recombinant E. coli, the increased flux toward UDP-glucose synthesis led to enhanced UDP-galactose-derived hyperoside synthesis. The efficiency of the recombinant strain was further improved by increasing the copy number of the PhUGT, which is a limiting step in the bioconversion. Through the optimization of the fermentation conditions, the production of hyperoside increased from 245.6 to 411.2 mg·L(−1). The production was also conducted using a substrate-fed batch fermentation, and the maximal hyperoside production was 831.6 mg·L(−1), with a molar conversion ratio of 90.2% and a specific productivity of 27.7 mg·L(−1)·h(−1) after 30 h of fermentation. The efficient hyperoside synthesis pathway described here can be used widely for the glycosylation of other flavonoids and bioactive substances. MDPI 2022-03-16 /pmc/articles/PMC8949062/ /pubmed/35336203 http://dx.doi.org/10.3390/microorganisms10030628 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 Li, Guosi Zhu, Fucheng Wei, Peipei Xue, Hailong Chen, Naidong Lu, Baowei Deng, Hui Chen, Cunwu Yin, Xinjian Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title | Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title_full | Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title_fullStr | Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title_full_unstemmed | Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title_short | Metabolic Engineering of Escherichia coli for Hyperoside Biosynthesis |
title_sort | metabolic engineering of escherichia coli for hyperoside biosynthesis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8949062/ https://www.ncbi.nlm.nih.gov/pubmed/35336203 http://dx.doi.org/10.3390/microorganisms10030628 |
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