Saved in:
Bibliographic Details
Main Authors: Moreno-Giménez, Elena, Morote, Lucía, Jiménez, Alberto José López, Parreño, Eduardo, Wang, Jian You, Nava, Matteo, Aguado, Carolina, Luján, Rafael, Al-Babili, Salim, Diretto, Gianfranco, Ahrazem, Oussama, Gómez-Gómez, Lourdes
Format: Artículo científico
Language:en
Published: The New phytologist 2026
Subjects:
Online Access:https://pubmed.ncbi.nlm.nih.gov/41889127/
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1868266069642182657
author Moreno-Giménez, Elena
Morote, Lucía
Jiménez, Alberto José López
Parreño, Eduardo
Wang, Jian You
Nava, Matteo
Aguado, Carolina
Luján, Rafael
Al-Babili, Salim
Diretto, Gianfranco
Ahrazem, Oussama
Gómez-Gómez, Lourdes
author_facet Moreno-Giménez, Elena
Morote, Lucía
Jiménez, Alberto José López
Parreño, Eduardo
Wang, Jian You
Nava, Matteo
Aguado, Carolina
Luján, Rafael
Al-Babili, Salim
Diretto, Gianfranco
Ahrazem, Oussama
Gómez-Gómez, Lourdes
Moreno-Giménez, Elena
Morote, Lucía
Jiménez, Alberto José López
Parreño, Eduardo
Wang, Jian You
Nava, Matteo
Aguado, Carolina
Luján, Rafael
Al-Babili, Salim
Diretto, Gianfranco
Ahrazem, Oussama
Gómez-Gómez, Lourdes
collection PubMed - marine biology
contents Bioconversion of carotenoids into high-value crocins using a marine sponge carotenoid cleavage dioxygenase. Moreno-Giménez, Elena Morote, Lucía Jiménez, Alberto José López Parreño, Eduardo Wang, Jian You Nava, Matteo Aguado, Carolina Luján, Rafael Al-Babili, Salim Diretto, Gianfranco Ahrazem, Oussama Gómez-Gómez, Lourdes Carotenoids Dioxygenases Animals Porifera Solanum lycopersicum Fruit Lycopene beta Carotene Pigmentation Escherichia coli Aquatic Organisms Carotenoids and apocarotenoids are widespread specialized metabolites, yet animals, including sponges, lack the ability to synthesize carotenoids de novo and must obtain them from dietary or microbial sources. The roles of carotenoid cleavage dioxygenases (CCDs) in marine animals remain largely unexplored. A CCD from the marine sponge Suberites domuncula (SdCDO) was evaluated for retinoid formation using a synthetic biology approach involving heterologous expression in Escherichia coli and tomato (Solanum lycopersicum), combined with metabolic, ultrastructural, and transcriptomic analyses. Unexpectedly, SdCDO did not produce retinoids. Instead, it cleaved lycopene and β-carotene to generate crocetin dialdehyde, the direct precursor of crocins. In tomato fruits, SdCDO expression triggered crocin accumulation, particularly in locular tissues, while reducing lycopene, lutein, and β-carotene levels. It also promoted the accumulation of upstream carotenoid intermediates, such as phytoene, phytofluene, and ζ-carotene. These metabolic changes resulted in orange fruit pigmentation and enhanced antioxidant capacity, along with altered chromoplast ultrastructure and broad downregulation of endogenous carotenoid biosynthetic genes. Overall, these findings reveal unexpected enzymatic plasticity in a sponge-derived CCD and demonstrate its ability to redirect plant carotenoid metabolism toward crocin biosynthesis. This work highlights the functional diversity of CCDs across kingdoms and their potential for synthetic biology and crop biofortification.
format Artículo científico
id pubmed_41889127
institution PubMed
language en
publishDate 2026
publisher The New phytologist
record_format pubmed
spellingShingle Bioconversion of carotenoids into high-value crocins using a marine sponge carotenoid cleavage dioxygenase.
Moreno-Giménez, Elena
Morote, Lucía
Jiménez, Alberto José López
Parreño, Eduardo
Wang, Jian You
Nava, Matteo
Aguado, Carolina
Luján, Rafael
Al-Babili, Salim
Diretto, Gianfranco
Ahrazem, Oussama
Gómez-Gómez, Lourdes
Carotenoids
Dioxygenases
Animals
Porifera
Solanum lycopersicum
Fruit
Lycopene
beta Carotene
Pigmentation
Escherichia coli
Aquatic Organisms
Bioconversion of carotenoids into high-value crocins using a marine sponge carotenoid cleavage dioxygenase. Moreno-Giménez, Elena Morote, Lucía Jiménez, Alberto José López Parreño, Eduardo Wang, Jian You Nava, Matteo Aguado, Carolina Luján, Rafael Al-Babili, Salim Diretto, Gianfranco Ahrazem, Oussama Gómez-Gómez, Lourdes Carotenoids Dioxygenases Animals Porifera Solanum lycopersicum Fruit Lycopene beta Carotene Pigmentation Escherichia coli Aquatic Organisms Carotenoids and apocarotenoids are widespread specialized metabolites, yet animals, including sponges, lack the ability to synthesize carotenoids de novo and must obtain them from dietary or microbial sources. The roles of carotenoid cleavage dioxygenases (CCDs) in marine animals remain largely unexplored. A CCD from the marine sponge Suberites domuncula (SdCDO) was evaluated for retinoid formation using a synthetic biology approach involving heterologous expression in Escherichia coli and tomato (Solanum lycopersicum), combined with metabolic, ultrastructural, and transcriptomic analyses. Unexpectedly, SdCDO did not produce retinoids. Instead, it cleaved lycopene and β-carotene to generate crocetin dialdehyde, the direct precursor of crocins. In tomato fruits, SdCDO expression triggered crocin accumulation, particularly in locular tissues, while reducing lycopene, lutein, and β-carotene levels. It also promoted the accumulation of upstream carotenoid intermediates, such as phytoene, phytofluene, and ζ-carotene. These metabolic changes resulted in orange fruit pigmentation and enhanced antioxidant capacity, along with altered chromoplast ultrastructure and broad downregulation of endogenous carotenoid biosynthetic genes. Overall, these findings reveal unexpected enzymatic plasticity in a sponge-derived CCD and demonstrate its ability to redirect plant carotenoid metabolism toward crocin biosynthesis. This work highlights the functional diversity of CCDs across kingdoms and their potential for synthetic biology and crop biofortification.
title Bioconversion of carotenoids into high-value crocins using a marine sponge carotenoid cleavage dioxygenase.
topic Carotenoids
Dioxygenases
Animals
Porifera
Solanum lycopersicum
Fruit
Lycopene
beta Carotene
Pigmentation
Escherichia coli
Aquatic Organisms
url https://pubmed.ncbi.nlm.nih.gov/41889127/