Phycocyanin (PC) is a soluble phycobiliprotein found within the light-harvesting phycobilisome complex of cyanobacteria and red algae, and is considered a high-value product due to its brilliant blue colour and fluorescent properties. However, commercially available PC has a relatively low temperature stability. Thermophilic species produce more thermostable variants of PC, but are challenging and energetically expensive to cultivate. Here, we show that the PC operon from the thermophilic cyanobacterium BP-1 () is functional in the mesophile sp. PCC 6803. Expression of in an 'Olive' mutant strain of lacking endogenous PC resulted in high yields of thermostable PC (112 ± 1 mg g DW) comparable to that of endogenous PC in wild-type cells. Heterologous PC also improved the growth of the Olive mutant, which was further supported by evidence of a functional interaction with the endogenous allophycocyanin core of the phycobilisome complex. The thermostability properties of the heterologous PC were comparable to those of PC from , and could be purified from the Olive mutant using a low-cost heat treatment method. Finally, we developed a scalable model to calculate the energetic benefits of producing PC from in cultures. Our model showed that the higher yields and lower cultivation temperatures of resulted in a 3.5-fold increase in energy efficiency compared to , indicating that producing thermostable PC in non-native hosts is a cost-effective strategy for scaling to commercial production.
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http://dx.doi.org/10.1016/j.mec.2021.e00175 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
State Key Laboratory of Protein and Plant Genetic Engineering, School of Life Science, Peking University, Beijing 100871, People's Republic of China.
Phycobilisomes (PBS) are the major photosynthetic light-harvesting complexes in cyanobacteria and red algae. While the structures of PBS have been determined in atomic resolutions, how PBS are attached to the reaction centers of photosystems remains less clear. Here, we report that a linker protein (LcpA) is required for the attachment of PBS to photosystem II (PSII) in the cyanobacterium sp.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Max Planck Institute for Medical Research, Jahnstr. 29, Heidelberg 69120, Germany.
Orange carotenoid protein (OCP) is a photoactive protein that mediates photoprotection in cyanobacteria. OCP binds different ketocarotenoid chromophores such as echinenone (ECN), 3'- hydroxyechinenone (hECN), and canthaxanthin (CAN). In the dark, OCP is in an inactive orange form known as OCP; upon illumination, a red active state is formed, referred to as OCP, that can interact with the phycobilisome.
View Article and Find Full Text PDFArch Microbiol
January 2025
Department of Botany, CMS College Kottayam, Kottayam, Kerala, 686001, India.
Among all photosynthetic life forms, cyanobacteria exclusively possess a water-soluble, light-sensitive carotenoprotein complex known as orange carotenoid proteins (OCPs), crucial for their photoprotective mechanisms. These protein complexes exhibit both structural and functional modularity, with distinct C-terminal (CTD) and N-terminal domains (NTD) serving as light-responsive sensor and effector regions, respectively. The majority of cyanobacterial genomes contain genes for OCP homologs and related proteins, highlighting their essential role in survival of the organism over time.
View Article and Find Full Text PDFPhotosynth Res
February 2025
Department of Biology, Washington University, St. Louis, MO, 63130, USA.
Excitation energy transfer between the photochemically active protein complexes is key for photosynthetic processes. Phototrophic organisms like cyanobacteria experience subtle changes in irradiance under natural conditions. Such changes need adjustments to the excitation energy transfer between the photosystems for sustainable growth.
View Article and Find Full Text PDFPhotosynthetica
December 2023
Centre Algatech, Institute of Microbiology of the Czech Academy of Sciences, Opatovický mlýn, 379 81 Třeboň, Czech Republic.
The investigation of spatial heterogeneity within the thylakoid membrane (TM) proteins has gained increasing attention in photosynthetic research. The recent advances in live-cell imaging have allowed the identification of heterogeneous organisation of photosystems in small cyanobacterial cells. These sub-micrometre TM regions, termed microdomains in cyanobacteria, exhibit functional similarities with granal (Photosystem II dominant) and stromal (Photosystem I dominant) regions observed in TM of higher plants.
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