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Molecules (Basel, Switzerland) Aug 2022Spirulina is a kind of blue-green algae (BGA) that is multicellular, filamentous, and prokaryotic. It is also known as a cyanobacterium. It is classified within the... (Review)
Review
Spirulina is a kind of blue-green algae (BGA) that is multicellular, filamentous, and prokaryotic. It is also known as a cyanobacterium. It is classified within the phylum known as blue-green algae. Despite the fact that it includes a high concentration of nutrients, such as proteins, vitamins, minerals, and fatty acids-in particular, the necessary omega-3 fatty acids and omega-6 fatty acids-the percentage of total fat and cholesterol that can be found in these algae is substantially lower when compared to other food sources. This is the case even if the percentage of total fat that can be found in these algae is also significantly lower. In addition to this, spirulina has a high concentration of bioactive compounds, such as phenols, phycocyanin pigment, and polysaccharides, which all take part in a number of biological activities, such as antioxidant and anti-inflammatory activity. As a result of this, spirulina has found its way into the formulation of a great number of medicinal foods, functional foods, and nutritional supplements. Therefore, this article makes an effort to shed light on spirulina, its nutritional value as a result of its chemical composition, and its applications to some food product formulations, such as dairy products, snacks, cookies, and pasta, that are necessary at an industrial level in the food industry all over the world. In addition, this article supports the idea of incorporating it into the food sector, both from a nutritional and health perspective, as it offers numerous advantages.
Topics: Dietary Supplements; Functional Food; Minerals; Phycocyanin; Spirulina
PubMed: 36080350
DOI: 10.3390/molecules27175584 -
Biochimica Et Biophysica Acta.... Apr 2020Cyanobacteria and red-algae share a common light-harvesting complex which is different than all other complexes that serve as photosynthetic antennas - the Phycobilisome... (Review)
Review
Cyanobacteria and red-algae share a common light-harvesting complex which is different than all other complexes that serve as photosynthetic antennas - the Phycobilisome (PBS). The PBS is found attached to the stromal side of thylakoid membranes, filling up most of the gap between individual thylakoids. The PBS self assembles from similar homologous protein units that are soluble and contain conserved cysteine residues that covalently bind the light absorbing chromophores, linear tetra-pyrroles. Using similar construction principles, the PBS can be as large as 16.8 MDa (68×45×39nm), as small as 1.2 MDa (24 × 11.5 × 11.5 nm), and in some unique cases smaller still. The PBS can absorb light between 450 nm to 650 nm and in some cases beyond 700 nm, depending on the species, its composition and assembly. In this review, we will present new observations and structures that expand our understanding of the distinctive properties that make the PBS an amazing light harvesting system. At the end we will suggest why the PBS, for all of its excellent properties, was discarded by photosynthetic organisms that arose later in evolution such as green algae and higher plants.
Topics: Bacterial Proteins; Energy Transfer; Light-Harvesting Protein Complexes; Models, Molecular; Photochemical Processes; Phycobilisomes
PubMed: 31306623
DOI: 10.1016/j.bbabio.2019.07.002 -
Biomolecules Nov 2019The phycobilisome (PBS) is the major light-harvesting complex of photosynthesis in cyanobacteria, red algae, and glaucophyte algae. In spite of the fact that it is very... (Review)
Review
The phycobilisome (PBS) is the major light-harvesting complex of photosynthesis in cyanobacteria, red algae, and glaucophyte algae. In spite of the fact that it is very well structured to absorb light and transfer it efficiently to photosynthetic reaction centers, it has been completely lost in the green algae and plants. It is difficult to see how selection alone could account for such a major loss. An alternative scenario takes into account the role of chance, enabled by (contingent on) the evolution of an alternative antenna system early in the diversification of the three lineages from the first photosynthetic eukaryote.
Topics: Bacterial Proteins; Chlorophyta; Cyanobacteria; Evolution, Molecular; Photosynthesis; Phycobilisomes; Plant Proteins; Rhodophyta
PubMed: 31752285
DOI: 10.3390/biom9110748 -
Marine Drugs Dec 2022Phycoerythrin (PE) is a pink/red-colored pigment found in rhodophytes, cryptophytes, and blue-green algae (cyanobacteria). The interest in PE is emerging from its role... (Review)
Review
Phycoerythrin (PE) is a pink/red-colored pigment found in rhodophytes, cryptophytes, and blue-green algae (cyanobacteria). The interest in PE is emerging from its role in delivering health benefits. Unfortunately, the current cyanobacterial-PE (C-PE) knowledge is still in the infant stage. It is essential to acquire a more comprehensive understanding of C-PE. This study aimed to review the C-PE structure, up and downstream processes of C-PE, application of C-PE, and strategies to enhance its stability and market value. In addition, this study also presented a strengths, weaknesses, opportunities, and threats (SWOT) analysis on C-PE. Cyanobacteria appeared to be the more promising PE producers compared to rhodophytes, cryptophytes, and macroalgae. Green/blue light is preferred to accumulate higher PE content in cyanobacteria. Currently, the prominent C-PE extraction method is repeated freezing-thawing. A combination of precipitation and chromatography approaches is proposed to obtain greater purity of C-PE. C-PE has been widely exploited in various fields, such as nutraceuticals, pharmaceuticals, therapeutics, cosmetics, biotechnology, food, and feed, owing to its bioactivities and fluorescent properties. This review provides insight into the state-of-art nature of C-PE and advances a step further in commercializing this prospective pigment.
Topics: Humans; Chromatography; Cyanobacteria; Phycoerythrin; Prospective Studies; Rhodophyta
PubMed: 36662201
DOI: 10.3390/md21010028 -
Molecular Microbiology Apr 2008Biliproteins are a widespread group of brilliantly coloured photoreceptors characterized by linear tetrapyrrolic chromophores, bilins, which are covalently bound to the... (Review)
Review
Biliproteins are a widespread group of brilliantly coloured photoreceptors characterized by linear tetrapyrrolic chromophores, bilins, which are covalently bound to the apoproteins via relatively stable thioether bonds. Covalent binding stabilizes the chromoproteins and is mandatory for phycobilisome assembly; and, it is also important in biliprotein applications such as fluorescence labelling. Covalent binding has, on the other hand, also considerably hindered biliprotein research because autocatalytic chromophore additions are rare, and information on enzymatic addition by lyases was limited to a single example, an EF-type lyase attaching phycocyanobilin to cysteine-alpha84 of C-phycocyanin. The discovery of new activities for the latter lyases, and of new types of lyases, have reinvigorated research activities in the subject. So far, work has mainly concentrated on cyanobacterial phycobiliproteins. Methodological advances in the process, however, as well as the finding of often large numbers of homologues, opens new possibilities for research on the subsequent assembly/disassembly of the phycobilisome in cyanobacteria and red algae, on the assembly and organization of the cryptophyte light-harvesting system, on applications in basic research such as protein folding, and on the use of phycobiliproteins for labelling.
Topics: Bacterial Proteins; Cyanobacteria; Phycobiliproteins; Protein Processing, Post-Translational; Rhodophyta
PubMed: 18284595
DOI: 10.1111/j.1365-2958.2008.06160.x -
Nature Communications Mar 2022Cyclophilins, or immunophilins, are proteins found in many organisms including bacteria, plants and humans. Most of them display peptidyl-prolyl cis-trans isomerase...
Cyclophilins, or immunophilins, are proteins found in many organisms including bacteria, plants and humans. Most of them display peptidyl-prolyl cis-trans isomerase activity, and play roles as chaperones or in signal transduction. Here, we show that cyclophilin anaCyp40 from the cyanobacterium Anabaena sp. PCC 7120 is enzymatically active, and seems to be involved in general stress responses and in assembly of photosynthetic complexes. The protein is associated with the thylakoid membrane and interacts with phycobilisome and photosystem components. Knockdown of anacyp40 leads to growth defects under high-salt and high-light conditions, and reduced energy transfer from phycobilisomes to photosystems. Elucidation of the anaCyp40 crystal structure at 1.2-Å resolution reveals an N-terminal helical domain with similarity to PsbQ components of plant photosystem II, and a C-terminal cyclophilin domain with a substrate-binding site. The anaCyp40 structure is distinct from that of other multi-domain cyclophilins (such as Arabidopsis thaliana Cyp38), and presents features that are absent in single-domain cyclophilins.
Topics: Cyanobacteria; Cyclophilins; Humans; Photosystem II Protein Complex; Phycobilisomes; Thylakoids
PubMed: 35354803
DOI: 10.1038/s41467-022-29211-w -
Nature Communications Jun 2022Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction...
Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction centers. PBSs are compositionally and structurally diverse, and exceedingly complex, all of which pose a challenge for a comprehensive understanding of their function. To date, three detailed architectures of PBSs by cryo-electron microscopy (cryo-EM) have been described: a hemiellipsoidal type, a block-type from rhodophytes, and a cyanobacterial hemidiscoidal-type. Here, we report cryo-EM structures of a pentacylindrical allophycocyanin core and phycocyanin-containing rod of a thermophilic cyanobacterial hemidiscoidal PBS. The structures define the spatial arrangement of protein subunits and chromophores, crucial for deciphering the energy transfer mechanism. They reveal how the pentacylindrical core is formed, identify key interactions between linker proteins and the bilin chromophores, and indicate pathways for unidirectional energy transfer.
Topics: Cryoelectron Microscopy; Cyanobacteria; Energy Transfer; Light-Harvesting Protein Complexes; Phycobilisomes; Rhodophyta
PubMed: 35715389
DOI: 10.1038/s41467-022-30962-9 -
Photosynthesis Research Aug 2018Cyanobacteria exhibit a novel form of non-photochemical quenching (NPQ) at the level of the phycobilisome. NPQ is a process that protects photosystem II (PSII) from... (Review)
Review
Cyanobacteria exhibit a novel form of non-photochemical quenching (NPQ) at the level of the phycobilisome. NPQ is a process that protects photosystem II (PSII) from possible highlight-induced photo-damage. Although significant advancement has been made in understanding the NPQ, there are still some missing details. This critical review focuses on how the orange carotenoid protein (OCP) and its partner fluorescence recovery protein (FRP) control the extent of quenching. What is and what is not known about the NPQ is discussed under four subtitles; where does exactly the site of quenching lie? (site), how is the quenching being triggered? (trigger), molecular mechanism of quenching (quenching) and recovery from quenching. Finally, a recent working model of NPQ, consistent with recent findings, is been described.
Topics: Cyanobacteria; Gene Expression Regulation, Bacterial; Photochemical Processes; Photosystem II Protein Complex; Phycobilisomes; Protein Conformation
PubMed: 29574660
DOI: 10.1007/s11120-018-0498-8 -
The FEBS Journal Aug 2022Blue-green algae, also known as cyanobacteria, contain some of the most efficient light-harvesting complexes known. These large, colourful complexes consist of...
Blue-green algae, also known as cyanobacteria, contain some of the most efficient light-harvesting complexes known. These large, colourful complexes consist of phycobiliproteins which are extremely valuable in the cosmetics, food, nutraceutical and pharmaceutical industries. Additionally, the colourful and fluorescent properties of phycobiliproteins can be modulated by metal ions, making them highly attractive as heavy metal sensors and heavy metal scavengers. Although the overall quenching ability metal ions have on phycobiliproteins is known, the mechanism of heavy metal binding to phycobiliproteins is not fully understood, limiting their widespread quantitative applications. Here, we show using high-resolution native mass spectrometry that phycobiliprotein complexes bind metal ions in different manners. Through monitoring the binding equilibria and metal-binding stoichiometry, we show in particular copper and silver to have drastic, yet different effects on phycobiliprotein structure, both copper and silver modulate the overall complex properties. Together, the data reveals the mechanisms by which metal ions can modulate phycobiliprotein properties which can be used as a basis for the future design of metal-related phycobiliprotein applications.
Topics: Copper; Cyanobacteria; Phycobiliproteins; Silver
PubMed: 35156751
DOI: 10.1111/febs.16396 -
Bioresource Technology Nov 2019Microalgae biorefinery systems have been extensively studied from the perspective of resources, energy expenditure, biofuel production potential, and high-added value... (Review)
Review
Microalgae biorefinery systems have been extensively studied from the perspective of resources, energy expenditure, biofuel production potential, and high-added value products. The genus Spirulina (Arthrospira) stands out among the microalgae of commercial importance. It accounts for over 30% of biomass produced globally because of high protein concentration and, carotenoid and phycocyanin content. Spirulina cultivation can be used to reduce greenhouse gases and for effluent treatment. Furthermore, its cellular morphology facilitates biomass recovery, which contributes to the process cost reduction. Spirulina biomass is widely applicable in food, feed, cosmetics, biofertilizers, biofuels, and biomaterials. A feasibility analysis of Spirulina biorefinery would provide specific information for the decision-making for the improvement of the Spirulina production process. In that context, this review aimed to present a parameter assessment to contribute to the economic viability of Spirulina production in a biorefinery system.
Topics: Biofuels; Biomass; Microalgae; Phycocyanin; Spirulina
PubMed: 31422868
DOI: 10.1016/j.biortech.2019.121946