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https://hdl.handle.net/1822/80401
Título: | Challenges in the heterologous production of furanocoumarins in Escherichia coli |
Autor(es): | Rodrigues, Joana Lúcia Lima Correia Gomes, Daniela Filipa Correia Rodrigues, L. R. |
Palavras-chave: | coumarins biosynthesis Escherichia coli heterologous production umbelliferone scopoletin esculetin p-coumaroyl-CoA 2'-hydroxylase prenyltransferase marmesin synthase psoralen synthase |
Data: | 25-Out-2022 |
Editora: | MDPI |
Revista: | Molecules |
Citação: | Rodrigues, J.L.; Gomes, D.; Rodrigues, L.R. Challenges in the Heterologous Production of Furanocoumarins in Escherichia coli. Molecules 2022, 27, 7230. https://doi.org/10.3390/molecules27217230 |
Resumo(s): | Coumarins and furanocoumarins are plant secondary metabolites with known biological activities. As they are present in low amounts in plants, their heterologous production emerged as a more sustainable and efficient approach to plant extraction. Although coumarins biosynthesis has been positively established, furanocoumarin biosynthesis has been far more challenging. This study aims to evaluate if Escherichia coli could be a suitable host for furanocoumarin biosynthesis. The biosynthetic pathway for coumarins biosynthesis in E. coli was effectively constructed, leading to the production of umbelliferone, esculetin and scopoletin (128.7, 17.6, and 15.7 µM, respectively, from tyrosine). However, it was not possible to complete the pathway with the enzymes that ultimately lead to furanocoumarins production. Prenyltransferase, psoralen synthase, and marmesin synthase did not show any activity when expressed in E. coli. Several strategies were tested to improve the enzymes solubility and activity with no success, including removing potential N-terminal transit peptides and expression of cytochrome P450 reductases, chaperones and/or enzymes to increase dimethylallylpyrophosphate availability. Considering the results herein obtained, E. coli does not seem to be an appropriate host to express these enzymes. However, new alternative microbial enzymes may be a suitable option for reconstituting the furanocoumarins pathway in E. coli. Nevertheless, until further microbial enzymes are identified, Saccharomyces cerevisiae may be considered a preferred host as it has already been proven to successfully express some of these plant enzymes. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/80401 |
DOI: | 10.3390/molecules27217230 |
ISSN: | 14203049 |
Versão da editora: | https://www.mdpi.com/1420-3049/27/21/7230 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_55830_1.pdf | 1,27 MB | Adobe PDF | Ver/Abrir |
Este trabalho está licenciado sob uma Licença Creative Commons