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Photochemical & Photobiological... Apr 2022Phycocyanobilin, the primary pigment of both light perception and light-harvesting in cyanobacteria, is synthesized from biliverdin IXα (BV) through intermediate 18,...
Phycocyanobilin, the primary pigment of both light perception and light-harvesting in cyanobacteria, is synthesized from biliverdin IXα (BV) through intermediate 18, 18-dihydrobiliverdin (18, 18-DHBV) by a phycocyanobilin:ferredoxin oxidoreductase (PcyA). In our previous study, we discovered two PcyA homologs (AmPcyAc and AmPcyAp) derived from Acaryochloris marina MBIC 11017 (A. marina) that exceptionally uses chlorophyll d as the primary photosynthetic pigment, absorbing longer wavelength far-red light than chlorophyll a, the photosynthetic pigment found in most cyanobacteria. Biochemical characterization of the two PcyA homologs identified functional diversification of these two enzymes: AmPcyAc provides 18, 18-DHBV, and PCB to the cyanobacteriochrome (CBCR) photoreceptors, whereas, AmPcyAp specifically provides PCB to the light-harvesting phycobilisome subunit. In this study, we focused on the residues necessary for 18, 18-DHBV supply to the CBCR photoreceptors by AmPcyAc. Based on the SyPcyA structure, we concentrated on the 30 residues that constitute the substrate-binding pocket. Among them, we discovered that Leu151 and Val225 in AmPcyAc were both substituted with isoleucine. During the enzymatic reaction, the SyPcyA variant molecule, possessing V225I and L151I replacements, accumulates the 18, 18-DHBV and supplies it to a CBCR molecule derived from A. marina. It is worth noting that the substitution of Val225 with isoleucine was specifically conserved among the Acaryochloris genus. Collectively, we propose that the specific evolution of PcyA among the Acaryochloris genus may correlate with the acquisition of Chl. d synthetic ability and growth in long-wavelength far-red light environments.
Topics: Chlorophyll; Chlorophyll A; Isoleucine; Oxidoreductases; Phycobilins; Phycocyanin
PubMed: 35394642
DOI: 10.1007/s43630-022-00198-z -
Bioresource Technology May 2022Microalgae are photosynthetic eukaryotes that serve as microbial cell factories for the production of useful biochemicals, including pigments. These pigments are... (Review)
Review
Microalgae are photosynthetic eukaryotes that serve as microbial cell factories for the production of useful biochemicals, including pigments. These pigments are eco-friendly alternatives to synthetic dyes and reduce environmental and health risks. They also exhibit excellent anti-oxidative properties, making them a useful commodity in the nutrition and pharmaceutical industries. Light-harvesting pigments such as chlorophylls and phycobilins, and photoprotective carotenoids are some of the most common microalgal pigments. The increasing demand for these pigments in industrial applications has prompted a need to improve their metabolic yield in microalgal cells. So far, expensive cultivation methods and sensitivity to microbial contamination remain the main obstacles to the large-scale production of these pigments. This review highlights current issues and future prospects related to the production of microalgal pigments. The review also emphasizes the use of engineering approaches such as genetic engineering, and optimization of media components and physical parameters to increase their commercial-scale production.
Topics: Biotechnology; Carotenoids; Chlorophyll; Genetic Engineering; Microalgae
PubMed: 35351568
DOI: 10.1016/j.biortech.2022.127071 -
Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae.ACS Central Science Mar 2022Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly...
Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly acting to absorb light where chlorophyll cannot (500-650 nm), phycobiliproteins also play an instrumental role in helping cryptophyte algae respond to changes in light intensity through the process of photoacclimation. Until recently, photoacclimation in cryptophyte algae was only observed as a change in the cellular concentration of phycobiliproteins; however, an additional photoacclimation response was recently discovered that causes shifts in the phycobiliprotein absorbance peaks following growth under red, blue, or green light. Here, we reproduce this newly identified photoacclimation response in two species of cryptophyte algae and elucidate the origin of the response on the protein level. We compare isolated native and photoacclimated phycobiliproteins for these two species using spectroscopy and mass spectrometry, and we report the X-ray structures of each phycobiliprotein and the corresponding photoacclimated complex. We find that neither the protein sequences nor the protein structures are modified by photoacclimation. We conclude that cryptophyte algae change one chromophore in the phycobiliprotein β subunits in response to changes in the spectral quality of light. Ultrafast pump-probe spectroscopy shows that the energy transfer is weakly affected by photoacclimation.
PubMed: 35350600
DOI: 10.1021/acscentsci.1c01209 -
Food & Function Mar 2022Phycocyanin is a typical microalgal active compound with antioxidant and anti-inflammatory efficacy, and the pigment moiety phycocyanobilin has been recently proposed as...
Phycocyanin is a typical microalgal active compound with antioxidant and anti-inflammatory efficacy, and the pigment moiety phycocyanobilin has been recently proposed as its active structural component. Here, to explore the structural basis for phycocyanin's intestinal protective action, we evaluated the therapeutic effects and mechanism of action of phycocyanin and phycocyanobilin in dextran sodium sulphate (DSS)-induced colitis mice and in Caco-2 and RAW 264.7 cells. Phycocyanobilin was obtained by solvothermal alcoholysis of phycocyanin and characterized by spectroscopy and mass spectrometry methods. Phycocyanin, phycocyanobilin and a positive drug mesalazine were intragastrically administered to C57BL/6 mice daily for 7 days during and after 4-day DSS exposure. Clinical signs and colon histopathology revealed that phycocyanin and phycocyanobilin had an equivalent anti-colitis efficacy that was even superior to mesalazine. Based on biochemical analysis of colonic tight junction proteins, mucus compositions and goblet cells, and colonic and peripheral proinflammatory cytokines, phycocyanin and phycocyanobilin displayed equivalent intestinal epithelial barrier-protecting and anti-inflammatory potential that was evidently superior to that of mesalazine. Flow cytometry analysis of phycocyanobilin fluorescence in Caco-2 cells unveiled a similar uptake efficacy of phycocyanin and phycocyanobilin by intestinal epithelial cells. According to lactic dehydrogenase release, 2',7'-dichlorodihydrofluorescein fluorescence and methylthiazolyldiphenyl-tetrazolium bromide assay in Caco-2 cells, phycocyanin and phycocyanobilin could equally and effectively protect the intestinal epithelial barrier from oxidant-induced disruption. Phycocyanin and phycocyanobilin also showed equivalent anti-inflammatory effects in tumor necrosis factor-α-stimulated Caco-2 cells and in lipopolysaccharides- and tumor necrosis factor-α-activated RAW264.7 cells. Overall, our results demonstrate the phycocyanobilin-dependent anti-colitis role of phycocyanin antioxidant and anti-inflammatory mechanisms.
Topics: Animals; Anti-Inflammatory Agents, Non-Steroidal; Antioxidants; Caco-2 Cells; Colitis; Epithelial Cells; Humans; Intestinal Mucosa; Male; Mesalamine; Mice; Mice, Inbred C57BL; Phycobilins; Phycocyanin; RAW 264.7 Cells
PubMed: 35244658
DOI: 10.1039/d1fo02970c -
Bioresource Technology May 2022Algae have been identified as natural producer of bioactive commercial pigments. To perform photosynthesis, algae use pigments to harvest sunlight energy. The pigments... (Review)
Review
Algae have been identified as natural producer of bioactive commercial pigments. To perform photosynthesis, algae use pigments to harvest sunlight energy. The pigments found in algae are categorized in chlorophylls, phycobilins, and carotenoids. Popular carotenoids include astaxanthin, lutein,fucoxanthin, canthaxanthin, zeaxanthin, β-cryptoxanthin and finds application as antioxidant, anti-inflammatory, immunoprophylactic, antitumor activities among others. Due to double-bonds in their structure, they exhibit broad health applications while protecting other molecules from oxidative stress induced by active radicals using various mechanisms. These carotenoids are synthesized by certain species as major products however they also present as byproducts in several species based on the pathway and genetic capability. Haematococcus pluvialis and Chlorella zofingiensis are ideal strains for commercial astaxanthin production. This review provides recent updates on microalgal pigment production, extraction, and purification processes to standardize and analyze for commercial production. Also, discussed the factors affecting its production, application, market potential, bottlenecks, and future prospects.
Topics: Carotenoids; Chlorella; Chlorophyceae; Lutein; Microalgae; Zeaxanthins
PubMed: 35231601
DOI: 10.1016/j.biortech.2022.126910 -
Microscopy and Microanalysis : the... Feb 2022Alga in the genus Chroothece have been reported mostly from aquatic or subaerial continental environments, where they grow in extreme conditions. The strain Chroothece...
Alga in the genus Chroothece have been reported mostly from aquatic or subaerial continental environments, where they grow in extreme conditions. The strain Chroothece mobilis MAESE 20.29 was exposed to different light intensities, red and green monochromatic light, ultraviolet (UV) radiation, high nitrogen concentrations, and high salinity to assess the effect of those environmental parameters on its growth. Confocal laser scanning microscopy (CLSM) was used as an “in vivo” noninvasive single-cell method for the study. The strain seemed to prefer fairly high light intensities and showed a significant increase in allophycocyanin (APC) and chlorophyll a [photosystem I (PSI) and photosystem II (PSII)] fluorescence with 330 and 789 μM/cm2/s intensities. Green monochromatic light promoted a significant increase in the fluorescence of APC and chlorophyll a (PSI and PSII). UV-A significantly decreased phycocyanin and increased APC, while UV-A + B showed a greater decreasing effect on c-Phycocyanin but did not significantly change concentrations of APC. The increase in nitrogen concentration in the culture medium significantly and negatively affected all pigments, and no effect was observed with an increase in salinity. Our data show that CLSM represents a very powerful tool for ecological research of microalgae in small volumes and may contribute to the knowledge of phycobiliproteins in vivo behavior and the parameters for the large-scale production of these pigments.
Topics: Chlorophyll; Chlorophyll A; Microscopy, Confocal; Photosystem I Protein Complex; Photosystem II Protein Complex; Rhodophyta
PubMed: 35177134
DOI: 10.1017/S1431927621013660 -
Analytical Biochemistry Apr 2022Cyanobacteriochromes are the extended family of phytochrome photosensors characterized in cyanobacteria. Alr1966g2C56A is a cyanobacteriochrome mutant of Alr1966g2 in...
Cyanobacteriochromes are the extended family of phytochrome photosensors characterized in cyanobacteria. Alr1966g2C56A is a cyanobacteriochrome mutant of Alr1966g2 in Nostoc sp. PCC 7120 from freshwater. In this paper, we truncated ten residues in the N-terminus and ten residues in the C-terminus of Alr1966g2C56A and obtained truncated Alr1966g2C46A, termed as Alr1966g2C46A-tr. Alr1966g2C46A-tr binded covalently not only phycocyanobilin but also biliverdin via Cys74 of the conserved CH motif, and showed a significant improvement in binding-PCB efficiency in E. coli, compared with that of untruncated Alr1966g2C56A. We also captured a persistent red fluorescence of Alr1966g2C46A-tr-PCB or Alr1966g2C46A-tr-BV expressed in live E. coli. Thus, Alr1966g2C46A-tr was suitable for the stable red fluorescent probe as a starting material.
Topics: Biliverdine; Cyanobacteria; Luminescent Proteins; Phycobilins; Phycocyanin; Phytochrome; Red Fluorescent Protein
PubMed: 35092720
DOI: 10.1016/j.ab.2022.114557 -
Photosynthesis Research Apr 2022Photosynthetic pigments are an integral and vital part of all photosynthetic machinery and are present in different types and abundances throughout the photosynthetic... (Review)
Review
Photosynthetic pigments are an integral and vital part of all photosynthetic machinery and are present in different types and abundances throughout the photosynthetic apparatus. Chlorophyll, carotenoids and phycobilins are the prime photosynthetic pigments which facilitate efficient light absorption in plants, algae, and cyanobacteria. The chlorophyll family plays a vital role in light harvesting by absorbing light at different wavelengths and allowing photosynthetic organisms to adapt to different environments, either in the long-term or during transient changes in light. Carotenoids play diverse roles in photosynthesis, including light capture and as crucial antioxidants to reduce photodamage and photoinhibition. In the marine habitat, phycobilins capture a wide spectrum of light and have allowed cyanobacteria and red algae to colonise deep waters where other frequencies of light are attenuated by the water column. In this review, we discuss the potential strategies that photosynthetic pigments provide, coupled with development of molecular biological techniques, to improve crop yields through enhanced light harvesting, increased photoprotection and improved photosynthetic efficiency.
Topics: Carotenoids; Chlorophyll; Cyanobacteria; Photosynthesis; Phycobilins; Plants
PubMed: 35064531
DOI: 10.1007/s11120-021-00892-6 -
Journal of Cell Science Dec 2021Near-infrared fluorescent protein (iRFP) is a bright and stable fluorescent protein with near-infrared excitation and emission maxima. Unlike the other conventional...
Near-infrared fluorescent protein (iRFP) is a bright and stable fluorescent protein with near-infrared excitation and emission maxima. Unlike the other conventional fluorescent proteins, iRFP requires biliverdin (BV) as a chromophore. Here, we report that phycocyanobilin (PCB) functions as a brighter chromophore for iRFP than BV, and that biosynthesis of PCB allows live-cell imaging with iRFP in the fission yeast Schizosaccharomyces pombe. We initially found that fission yeast cells did not produce BV and therefore did not show any iRFP fluorescence. The brightness of iRFP-PCB was higher than that of iRFP-BV both in vitro and in fission yeast. We introduced SynPCB2.1, a PCB biosynthesis system, into fission yeast, resulting in the brightest iRFP fluorescence. To make iRFP readily available in fission yeast, we developed an endogenous gene tagging system with iRFP and all-in-one integration plasmids carrying the iRFP-fused marker proteins together with SynPCB2.1. These tools not only enable the easy use of multiplexed live-cell imaging in fission yeast with a broader color palette, but also open the door to new opportunities for near-infrared fluorescence imaging in a wider range of living organisms. This article has an associated First Person interview with the first author of the paper.
Topics: Humans; Luminescent Proteins; Phycobilins; Phycocyanin; Schizosaccharomyces
PubMed: 34806750
DOI: 10.1242/jcs.259315 -
Journal of Agricultural and Food... Nov 2021Phycoerythrin (PE) is a natural water-soluble pigment protein with characteristic phycobilins and is sensitive to thermal and light environmental changes. In this study,...
Phycoerythrin (PE) is a natural water-soluble pigment protein with characteristic phycobilins and is sensitive to thermal and light environmental changes. In this study, PE was extracted from and PE-oligochitosan complexes (POC) were fabricated by a self-assembly approach. The effects of cationic oligochitosan on the binding interaction, structure, size distribution, and color stability of PE were evaluated. The stoichiometric number was calculated to be 21.67 ± 2.65 (oligochitosan/PE) and the binding constant K was (6.47 ± 0.48) × 10 M. Cationic oligochitosan could electrostatically interact with PE and affect the PE structure by increasing the α-helix content. In addition, high concentrations of oligochitosan led to the formation of dense phycoerythrin protein granules. Moreover, at a reaction ratio of 20.0:1 (oligochitosan/PE), being approximately the predicted stoichiometric number , the thermal stability (40-80 °C), natural light stability, and ultraviolet light irradiation (254 nm) stability of the POC were improved. This study provides an approach to reduce the susceptibility of PE upon environmental changes by forming a stable self-assembly complex, which will promote the application of PE as a natural pigment protein in food and chemical applications.
Topics: Chitin; Chitosan; Oligosaccharides; Phycoerythrin; Rhodophyta; Static Electricity
PubMed: 34669400
DOI: 10.1021/acs.jafc.1c05205