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Molecules (Basel, Switzerland) Sep 2022Phycocyanin is a blue fluorescent protein with multi-bioactive functions. However, the multi-bioactivities and spectral stability of phycocyanin are susceptible to... (Review)
Review
Phycocyanin is a blue fluorescent protein with multi-bioactive functions. However, the multi-bioactivities and spectral stability of phycocyanin are susceptible to external environmental conditions, which limit its wide application. Here, the structure, properties, and biological activity of phycocyanin were discussed. This review highlights the significance of the microcapsules' wall materials which commonly protect phycocyanin from environmental interference and summarizes the current preparation principles and characteristics of microcapsules in food and pharma industries, including spray drying, electrospinning, electrospraying, liposome delivery, sharp-hole coagulation baths, and ion gelation. Moreover, the major technical challenge and corresponding countermeasures of phycocyanin microencapsulation are also appraised, providing insights for the broader application of phycocyanin.
Topics: Capsules; Liposomes; Phycocyanin
PubMed: 36144588
DOI: 10.3390/molecules27185854 -
Biochemical Society Transactions Dec 2020Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood... (Review)
Review
Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10-18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.
Topics: Animals; Anthozoa; Biliverdine; Biophysics; Biosensing Techniques; Cyanobacteria; Fluorescent Dyes; Green Fluorescent Proteins; Humans; Hydrogen Peroxide; Luminescent Proteins; Mice; Nanoparticles; Neoplasms; Oxygen; Photobleaching; Phycobilisomes; Phytochrome; Scattering, Radiation; Spectrometry, Fluorescence; Trichodesmium; Red Fluorescent Protein
PubMed: 33196077
DOI: 10.1042/BST20200444 -
Marine Drugs Oct 2023Phycobiliproteins (PBPs) are natural water-soluble pigment proteins, which constitute light-collecting antennae, and function in algae photosynthesis, existing in... (Review)
Review
Phycobiliproteins (PBPs) are natural water-soluble pigment proteins, which constitute light-collecting antennae, and function in algae photosynthesis, existing in cyanobacteria, red algae, and cryptomonads. They are special pigment-protein complexes in algae with a unique structure and function. According to their spectral properties, PBPs can be mainly divided into three types: allophycocyanin, phycocyanin, and PE. At present, there are two main sources of PBPs: one is natural PBPs extracted from algae and the other way is recombinant PBPs which are produced in engineered microorganisms. The covalent connection between PBP and streptavidin was realized by gene fusion. The bridge cascade reaction not only improved the sensitivity of PBP as a fluorescent probe but also saved the preparation time of the probe, which expands the application range of PBPs as fluorescent probes. In addition to its function as a light-collecting antenna in photosynthesis, PBPs also have the functions of biological detection, ion detection, and fluorescence imaging. Notably, increasing studies have designed novel PBP-based far-red fluorescent proteins, which enable the tracking of gene expression and cell fate.
Topics: Phycobiliproteins; Fluorescent Dyes; Photosynthesis
PubMed: 37999396
DOI: 10.3390/md21110572 -
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 -
Marine Drugs Jul 2022Phycobiliproteins (PBPs) are colored and water-soluble biliproteins found in cyanobacteria, rhodophytes, cryptomonads and cyanelles. They are divided into three main... (Review)
Review
Phycobiliproteins (PBPs) are colored and water-soluble biliproteins found in cyanobacteria, rhodophytes, cryptomonads and cyanelles. They are divided into three main types: allophycocyanin, phycocyanin and phycoerythrin, according to their spectral properties. There are two methods for PBPs preparation. One is the extraction and purification of native PBPs from Cyanobacteria, Cryptophyta and Rhodophyta, and the other way is the production of recombinant PBPs by heterologous hosts. Apart from their function as light-harvesting antenna in photosynthesis, PBPs can be used as food colorants, nutraceuticals and fluorescent probes in immunofluorescence analysis. An increasing number of reports have revealed their pharmaceutical potentials such as antioxidant, anti-tumor, anti-inflammatory and antidiabetic effects. The advances in PBP biogenesis make it feasible to construct novel PBPs with various activities and produce recombinant PBPs by heterologous hosts at low cost. In this review, we present a critical overview on the productions, characterization and pharmaceutical potentials of PBPs, and discuss the key issues and future perspectives on the exploration of these valuable proteins.
Topics: Cryptophyta; Cyanobacteria; Pharmaceutical Preparations; Phycobiliproteins; Phycoerythrin; Rhodophyta
PubMed: 35877743
DOI: 10.3390/md20070450 -
Photosynthesis Research Aug 2020The major light-harvesting system in cyanobacteria, the phycobilisome, is an essential component of the photosynthetic apparatus that regulates the utilization of the...
The major light-harvesting system in cyanobacteria, the phycobilisome, is an essential component of the photosynthetic apparatus that regulates the utilization of the natural light source-the Sun. Earlier works revealed that the thylakoid membrane composition and its physical properties might have an important role in antennas docking. Polyunsaturated lipids and xanthophylls are among the most significant modulators of the physical properties of thylakoid membranes. In the nature, the action of these molecules is orchestrated in response to environmental stimuli among which the growth temperature is the most influential. In order to further clarify the significance of thylakoid membrane physical properties for the phycobilisomes assembly (i.e. structural integrity) and their ability to efficiently direct the excitation energy towards the photosynthetic complexes, in this work, we utilize cyanobacterial Synechocystis sp. PCC 6803 mutants deficient in polyunsaturated lipids (AD mutant) and xanthophylls (RO mutant), as well as a strain depleted of both xanthophylls and polyunsaturated lipids (ROAD multiple mutant). For the first time, we discuss the effect of those mutations on the phycobilisomes assembly, integrity and functionality at optimal (30 °C) and moderate low (25 °C) and high (35 °C) temperatures. Our results show that xanthophyll depletion exerts a much stronger effect on both phycobilisome's integrity and the response of cells to growth at suboptimal temperatures than lipid unsaturation level. The strongest effects were observed for the combined ROAD mutant, which exhibited thermally destabilized phycobilisomes and a population of energetically uncoupled phycocyanin units.
Topics: Carotenoids; Lipid Metabolism; Mutation; Photosynthesis; Photosynthetic Reaction Center Complex Proteins; Phycobilisomes; Phycocyanin; Synechocystis; Temperature; Thylakoids; Xanthophylls
PubMed: 32720110
DOI: 10.1007/s11120-020-00776-1 -
Analytical Biochemistry Dec 2022Single-molecule methods, specifically single-molecule counting, convey high sensitivity in research applications. However, single-molecule counting experiments require...
Single-molecule methods, specifically single-molecule counting, convey high sensitivity in research applications. However, single-molecule counting experiments require specialized equipment or consumables to perform. We demonstrate the utility of using bright Streptavidin-Phycoerythrin (SA-PE) conjugates and an epifluorescence microscope, for single-molecule counting applications. In this work, we show that we can visualize single-molecules on glass surfaces, perform single-molecule diagnostic assays on magnetic microparticles, and image individual foci on cell surfaces. This approach is simple and effective for researchers interested in single-molecule counting.
Topics: Streptavidin; Phycoerythrin; Nanotechnology; Magnetics
PubMed: 36265689
DOI: 10.1016/j.ab.2022.114955 -
Journal of Visualized Experiments : JoVE Feb 2023Red algae (Rhodophyta) contain phycobiliproteins and colonize habitats with dim light, however some (e.g., some Chroothece species) can also develop in full sunshine....
Red algae (Rhodophyta) contain phycobiliproteins and colonize habitats with dim light, however some (e.g., some Chroothece species) can also develop in full sunshine. Most rhodophytes are red, however some can appear bluish, depending on the proportion of blue and red biliproteins (phycocyanin and phycoerythrin). Different phycobiliproteins can capture light at diverse wavelengths and transmit it to chlorophyll a, which makes photosynthesis under very different light conditions possible. These pigments respond to habitat changes in light, and their autofluorescence can help to study biological processes. Using Chroothece mobilis as a model organism and the spectral lambda scan mode in a confocal microscope, the adaptation of photosynthetic pigments to different monochromatic lights was studied at the cellular level to guess the species' optimal growth conditions. The results showed that, even when the studied strain was isolated from a cave, it adapted to both dim and medium light intensities. The presented method is especially useful for studying photosynthetic organisms that do not grow or grow very slowly under laboratory conditions, which is usually the case for those living in extreme habitats.
Topics: Chlorophyll A; Optical Imaging; Acclimatization; Caves; Phycobiliproteins
PubMed: 36876941
DOI: 10.3791/64533 -
The Science of the Total Environment Nov 2021Bio-removal of negative charged platinum complex is of great challenge owing to electrostatic repulsions between PtCl and general extracellular polymeric substance (EPS)...
Bio-removal of negative charged platinum complex is of great challenge owing to electrostatic repulsions between PtCl and general extracellular polymeric substance (EPS) of microorganism. Galdieria sulphuraria (GS) are thermophilic and acidophilic microalga with specific metabolism, which subsequently lead to their unique cellular compositions such as EPS and phycocyanin, possibly providing a strategy to deal with negative charged metal complex. Accordingly, G. sulphuraria are employed to remove negative charged PtCl complex with initial concentrations ranging from 0, 10, 20, 30, to 45 ppm. The growth rates of G. sulphuraria with microalgae named as GS-0, GS-10, GS-20, GS-30, and GS-45, respectively, and simultaneously bio-removal efficiencies of PtCl are investigated. G. sulphuraria are independent to PtCl within 0-30 ppm, while they are inhibited within 45 ppm of PtCl. The PtCl removal efficiencies of GS-10, GS-20, and GS-30 increase from 94.58%, 95.52%, to 95.92%, while decrease to 71.81% of GS-45. About 92.39%, 93.77%, 94.29%, and 75.21% of PtCl adsorbed are accumulated within GS-10, GS-20, GS-30, GS-45, with few in EPS. The PtCl complexes accumulated in EPS and algae cells are possibly decomposed to PtCl according to the increasing zeta potentials of EPS and algae cells. The results indicate that PtCl is efficiently removed by G. sulphuraria, achieving bio-removal of negative charged PtCl complex from wastewater.
Topics: Extracellular Polymeric Substance Matrix; Microalgae; Phycocyanin; Rhodophyta; Wastewater
PubMed: 34280622
DOI: 10.1016/j.scitotenv.2021.149021 -
Food Research International (Ottawa,... May 2021Phycocyanin (C-PC) application by the industry is still limited due to extraction methods drawbacks and to the low stability of these compounds after the extraction... (Review)
Review
Phycocyanin (C-PC) application by the industry is still limited due to extraction methods drawbacks and to the low stability of these compounds after the extraction process. To overcome such limitations, alternative extraction methodologies have been evaluated, and stabilizing agents have been used under different conditions in the past years. Therefore, the aim of this review was to bring the state of the art of C-PC extraction methods, including main parameters that affect the extraction process and cell disruption mechanisms, as well as the physical and chemical parameters that may influence C-PC stability. Stabilizing agents have been used to avoid C-PC content degradation during storage and food processing. A critical analysis of the extraction methods indicated that pulsed electric field (PEF) is a promising technology for C-PC extraction since the extracts present relative high C-PC concentration and purity. Other methods either result in low purity extracts or are time demanding. Regarding stabilizing agents, natural polymers and sugars are potential compounds to be used in food formulations to avoid color and antioxidant activity losses.
Topics: Animals; Antioxidants; Decapodiformes; Food Handling; Phycocyanin; Spirulina
PubMed: 33992333
DOI: 10.1016/j.foodres.2021.110314