ArticleBMC biotechnology2012
Scalable production of biliverdin IXα by Escherichia coli.
Article in BMC biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 37 citations in OpenAlex.
- Systemic engineering and global regulation enabling high-level bilirubin biosynthesis.Nature communications · 2025Article
- An Alternative to Biliverdin, Mesobiliverdin IXα and Mesobiliverdin-Enriched Microalgae: A Review on the Production and Applications of Mesobiliverdin-Related Products.Molecules (Basel, Switzerland) · 2025Review
- Systems metabolic engineering ofFrontiers in plant science · 2025Article
- Optimization of Phycocyanobilin Synthesis inGenes · 2024Article
- Production of biliverdin by biotransformation of exogenous heme using recombinant Pichia pastoris cells.Bioresources and bioprocessing · 2024Article
- Multi-omics revealed rumen microbiota metabolism and host immune regulation in Tibetan sheep of different ages.Frontiers in microbiology · 2024Article
- Improvement in bilirubin influence on cholesterol efflux capacity evaluation using the immobilized liposome-bound gel beads method.Bioscience reports · 2023Article
- Production of bilirubin by biotransformation of biliverdin using recombinant Escherichia coli cells.Bioprocess and biosystems engineering · 2022Article
- Bilirubin as a Therapeutic Molecule: Challenges and Opportunities.Antioxidants (Basel, Switzerland) · 2021Review
- Recombinant Production of Biliverdin IXβ and δ Isomers in the T7 Promoter CompatibleFrontiers in microbiology · 2021Article
- Imaging living obligate anaerobic bacteria with bilin-binding fluorescent proteins.Current research in microbial sciences · 2020Article
- Systems metabolic engineering ofJournal of biological engineering · 2019Article
- Identification of a biliverdin geometric isomer by means of HPLC/ESI-MS and NMR spectroscopy. Differentiation of the isomers by using fragmentation "in-source".Monatshefte fur chemie · 2018Article
- Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2016Article
- An infrared reporter to detect spatiotemporal dynamics of protein-protein interactions.Nature methods · 2014Article
- Mesobiliverdin IXα Enhances Rat Pancreatic Islet Yield and Function.Frontiers in pharmacology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBiliverdin IXα is produced when heme undergoes reductive ring cleavage at the α-methene bridge catalyzed by heme oxygenase. It is subsequently reduced by biliverdin reductase to bilirubin IXα which is a potent endogenous antioxidant. Biliverdin IXα, through interaction with biliverdin reductase, also initiates signaling pathways leading to anti-inflammatory responses and suppression of cellular pro-inflammatory events. The use of biliverdin IXα as a cytoprotective therapeutic has been suggested, but its clinical development and use is currently limited by insufficient quantity, uncertain purity, and derivation from mammalian materials. To address these limitations, methods to produce, recover and purify biliverdin IXα from bacterial cultures of Escherichia coli were investigated and developed.
resultsRecombinant E. coli strains BL21(HO1) and BL21(mHO1) expressing cyanobacterial heme oxygenase gene ho1 and a sequence modified version (mho1) optimized for E. coli expression, respectively, were constructed and shown to produce biliverdin IXα in batch and fed-batch bioreactor cultures. Strain BL21(mHO1) produced roughly twice the amount of biliverdin IXα than did strain BL21(HO1). Lactose either alone or in combination with glycerol supported consistent biliverdin IXα production by strain BL21(mHO1) (up to an average of 23. 5mg L(-1) culture) in fed-batch mode and production by strain BL21 (HO1) in batch-mode was scalable to 100L bioreactor culture volumes. Synthesis of the modified ho1 gene protein product was determined, and identity of the enzyme reaction product as biliverdin IXα was confirmed by spectroscopic and chromatographic analyses and its ability to serve as a substrate for human biliverdin reductase A.
conclusionsMethods for the scalable production, recovery, and purification of biliverdin IXα by E. coli were developed based on expression of a cyanobacterial ho1 gene. The purity of the produced biliverdin IXα and its ability to serve as substrate for human biliverdin reductase A suggest its potential as a clinically useful therapeutic.
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