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Phycocyanin

phycocyanin benefits, phycocyanin
Phycocyanin is a pigment-protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin[1] It is an accessory pigment to chlorophyll All phycobiliproteins are water-soluble, so they cannot exist within the membrane like carotenoids can Instead, phycobiliproteins aggregate to form clusters that adhere to the membrane called phycobilisomes Phycocyanin is a characteristic light blue color, absorbing orange and red light, particularly near 620 nm depending on which specific type it is, and emits fluorescence at about 650 nm also depending on which type it is Allophycocyanin absorbs and emits at longer wavelengths than phycocyanin C or phycocyanin R Phycocyanins are found in Cyanobacteria also called blue-green algae Phycobiliproteins have fluorescent properties that are used in immunoassay kits Phycocyanin is from the Greek phyco meaning “algae” and cyanin is from the English word “cyan", which conventionally means a shade of blue-green close to "aqua" and is derived from the Greek “kyanos" which means a somewhat different color: "dark blue" The product phycocyanin, produced by Aphanizomenon flos-aquae and Spirulina, is for example used in the food and beverage industry as the natural coloring agent 'Lina Blue' or 'EXBERRY Shade Blue' and is found in sweets and ice cream In addition, fluorescence detection of phycocyanin pigments in water samples is a useful method to monitor cyanobacteria biomass[2]

The phycobiliproteins are made of two subunitsalpha and beta having a protein backbone to which 1-2 linear tetrapyrrole chromophores are covalently bound

C-phycocyanin is often found in cyanobacteria which thrive around hot springs, as it can be stable up to around 70 °C, with identical spectroscopic light absorbing behaviours at 20 and 70 °C Thermophiles contain slightly different amino acid sequences making it stable under these higher conditions Molecular weight is around 30,000 Da Stability of this protein invitro at these temperatures has been shown to be substantially lower Photo-spectral analysis of the protein after 1 min exposure to 65 °C conditions in a purified state demonstrated a 50% loss of tertiary structure

Phycocyanin pigment extracted from Microcystis aeruginosa cyanobacteria

Contents

  • 1 Structure
  • 2 Spectral characteristics
  • 3 Ecological Relevance
  • 4 Biosynthesis
  • 5 Biotechnology
    • 51 Applications
    • 52 Medicine
      • 521 Anti-oxidation and Anti-inflammation
      • 522 Neuroprotection
      • 523 Hepatoprotection
      • 524 Anti-cancer
    • 53 Food
  • 6 References
  • 7 Further reading

Structure

Phycocyanin αβ monomer Phycocyanin αβ6 hexamer

Phycocyanin shares a common structural theme with all phycobiliproteins[3] The structure begins with the assembly of phycobiliprotein monomers, which are heterodimers composed of α and β subunits, and their respective chromophores linked via thioether bond

Each subunit is typically composed of eight α-helices Monomers spontaneously aggregate to form ring-shaped trimers αβ3, which have rotational symmetry and a central channel Trimers aggregate in pairs to form hexamers αβ6, sometimes assisted with additional linker proteins Each phycobilisome rod generally has two or more phycocyanin hexamers Despite the overall similarity in structure and assembly of phycobiliproteins, there is a large diversity in hexamer and rod conformations, even when only considering phycocyanins On a larger scale phycocyanins also vary in crystal structure, although the biological relevance of this is debatable

As an example, the structure of C-phycocyanin from Synechococcus vulcanus has been refined to 16 Angstrom resolution[4] The αβ monomer consists of 332 amino acids and 3 thio-linked phycocyanobilin PCB cofactor molecules Both the α- and β-subunits have a PCB at amino acid 84, but the β-subunit has an additional PCB at position 155 as well This additional PCB faces the exterior of the trimeric ring and is therefore implicated in inter-rod energy transfer in the phycobilisome complex In addition to cofactors, there are many predictable non-covalent interactions with the surrounding solvent water that are hypothesized to contribute to structural stability

R-phycocyanin II R-PC II is found in some Synechococcus species[5] R-PC II is said to be the first PEB containing phycocyanin that originates in cyanobacteria[5] Its purified protein is composed of alpha and beta subunits in equal quantities[5] R-PC II has PCB at beta-84 and the phycoerythrobillin PEB at alpha-84 and beta-155[5]

As of March 7, 2018, there are 44 crystal structures of phycocyanin deposited in the Protein Data Bank[6]

Spectral characteristics

C-phycocyanin has a single absorption peak at ~621 nm,[7][8] varying slightly depending on the organism and conditions such as temperature, pH, and protein concentration in vitro[9][10] Its emission maximum is ~642 nm[7][8] This means that the pigment absorbs orange light, and emits reddish light R-phycocyanin has an absorption maxima at 533 and 544 nm[5] The fluorescence emission maximum of R-phycocyanin is 646 nm[5]

Property C-Phycocyanin R-Phycocyanin
Absorption maximum nm 621 533, 544
Emission maximum nm 642 646
Extinction Coefficient ε 154x106 M−1cm−1 -
Quantum Yield 081 -

Ecological Relevance

Phycocyanin is produced by many photoautotrophic cyanobacteria[11] Even if cyanobacteria have large concentrations of phycocyanin, productivity in the ocean is still limited due to light conditions[11]

Phycocyanin has ecological significance in indicating cyanobacteria bloom Normally chlorophyll a is used to indicate cyanobacteria numbers, however since it is present in a large number of phytoplankton groups, it is not an ideal measure[12] For instance a study in the Baltic Sea used phycocyanin as a marker for filamentous cyanobacteria during toxic summer blooms[12] Some filamentous organisms in the Baltic Sea include Nodularia spumigena and Aphanizomenon flosaquae

An important cyanobacteria named spirulina Arthrospira plantensis is a micro algae that produces C-PC[13]

There are many different methods of phycocyanin production including photoautotrophic, mixotrophic and heterotrophic and recombinant production[14] Photoautotrophic production of phycocyanin is where cultures of cyanobacteria are grown in open ponds in either subtropical or tropical regions[14] Mixotrophic production of algae is where the algae are grown on cultures that have an organic carbon source like glucose[14] Using mixotrophic production produces higher growth rates and higher biomass compared to simply using a photoautotrophic culture[14] In the mixotrophic culture, the sum of heterotrophic and autotrophic growth separately was equal to the mixotrophic growth[15] Heterotrophic production of phycocyanin is not light limited, as per its definition[14] Galdieria sulphuraria is a unicellular rhodophyte that contains a large amount of C-PC and a small amount of allophycocyanin[14] G sulphuraria is an example of the heterotrophic production of C-PC because its habitat is hot, acidic springs and uses a number of carbon sources for growth[14] Recombinant production of C-PC is another heterotrophic method and involves gene engineering[14]

Lichen-forming fungi and cyanobacteria often have a symbiotic relationship and thus phycocyanin markers can be used to show the ecological distribution of fungi-associated cyanobacteria As shown in the highly specific association between Lichina species and Rivularia strains, phycocyanin has enough phylogenetic resolution to resolve the evolutionary history of the group across the northwestern Atlantic ocean coastal margin[16]

Biosynthesis

The two genes cpcA and cpcB, located in the cpc operon and translated from the same mRNA transcript, encode for the C-PC α- and β-chains respectively[17] Additional elements such as linker proteins, and enzymes involved in phycobilin synthesis and the phycobiliproteins are often encoded by genes in adjacent gene clusters, and the cpc operon of Arthrospira platensis also encodes a linker protein assisting in the assembly of C-PC complexes[18] In red algae, the phycobiliprotein and linker protein genes are located on the plastid genome[19]

Phycocyanobilin is synthesised from heme and inserted into the C-PC apo-protein by three enzymatic steps[20] Cyclic heme is oxidised to linear biliverdin IXα by heme oxygenase and further converted to 3Z-phycocyanobilin, the dominant phycocyanobilin isomer, by 3Z-phycocyanobilin:ferredoxin oxidoreductase Insertion of 3Z-phycocyanobilin into the C-PC apo-protein via thioether bond formation is catalysed by phycocyanobilin lyase[21]

The promoter for the cpc operon is located within the 427-bp upstream region of the cpcB gene In A platensis, 6 putative promoter sequences have been identified in the region, with four of them showing expression of green fluorescent protein when transformed into E coli[22] The presence of other positive elements such as light-response elements in the same region have also been demonstrated[23]

The multiple promoter and response element sequences in the cpc operon enable cyanobacteria and red algae to adjust its expression in response to multiple environmental conditions Expression of the cpcA and cpcB genes is regulated by light Low light intensities stimulate synthesis of CPC and other pigments, while pigment synthesis is repressed at high light intensities[24] Temperature has also been shown to affect synthesis, with specific pigment concentrations showing a clear maximum at 36 °C in Arthronema africanum, a cyanobacterium with particular high C-PC and APC contents[25]

Nitrogen and also iron limitation induce phycobiliprotein degradation Organic carbon sources stimulate C-PC synthesis in Anabaena spp, but seem to have almost no effector negative effect in A platensis[26][27] In the rhodophytes Cyanidium caldarium and Galdieria sulphuraria, C-PC production is repressed by glucose but stimulated by heme[28]

Biotechnology

Pure phycocyanin extractions can be isolated from algae The basic segregation order is as followed The rupturing of the cell wall, with mechanical forces freeze thawing or chemical agents enzymes Then, C-PC is isolate with centrifugation and purified with ammonium sulfate precipitation or chromotography -either ion or gel-filtration After, the sample gets frozen and dried[14]

Applications

Phycocyanin can be used in many practices, it is particularly used medicine and foods applications It can also be used in genetics, where it acts a tracer due to its natural fluorescence[29]

Medicine

Anti-oxidation and Anti-inflammation

Phycocyanin has both anti-oxidant and anti-inflammation properties[30][31][32] Peroxyl, hydroxyl, and alkoxyl radicals are all oxidants scavenged by C-PC C-PC, however, has a greater effect on peroxyl radicals C-PC is a metal binding antioxidant as it prevents lipid peroxidation from occurring[33] The peroxyl radicals are stabilized by the chromophore a subunit of C-PC[34] For hydroxyl radicals to be scavenged, it must be done in low light and with high C-PC levels[35] Hydroxyl radicals are found at inflamed parts of the body[33] C-PC, being an anti-oxidant, scavenges these damage-inducing radicals, hence being an anti-inflammation agent

Neuroprotection

Excess oxygen in the brain generates Reactive Oxygen Species ROS ROS causes damages to brain neurons, leading to strokes C-phycocyanin scavenges hydrogen peroxide, a type of ROS species, from the inside of astrocyte, reducing oxidative stress[36] Astrocytes also increase the production of growth factors like BDNF and NDF, therefore, enhance nerve regeneration C-PC also prevents astrogliosis and glial inflammation[36][37]

Hepatoprotection

C-phycocyanin is found to have hepatotoxicity protection[30][38] Vadiraja et al 1998 found an increase in the serum glutamic pyruvic transaminase SGPT when C-PC is treated against heptatoxins such as Carbon tetrachloride CCl4 or R-+-pulegone C-PC protects the liver by the means of the Cytochrome-P450 system[38] It can either disturb the production of menthofuran or disturb formation of α, β-unsaturated- γ-ketoaldehyde Both of which are key components of the cytochrome P-450 system that produced a reactive metabolite that produce toxins when it binds to liver tissues Another possible protection mechanism by C-PC can be the scavenging of reactive metabolites or free radicals if the cause is CCl4

Anti-cancer

C-phycocyanin C-PC has anti-cancer effects Cancer happens when cells continue to grow uncontrollably C-PC has been found to prevent cell growth[39] C-PC stops the formation of tumour before the S phase DNA synthesis is not performed due to the tumour cell entering G0, resulting in no tumour proliferation[40] Furthermore, C-PC induces apoptosis When cells are treated with C-PC, ROS Radical Oxygen Species are made These molecules decrease BCl-2 regulator of apoptosis production Here, BCl-2 inhibits proteins called caspases Caspases are part of the apoptosis pathway When BCl-2 decreases, the expression of caspases increases As a result, apoptosis occurs[41][40] C-PC alone is not enough to treat cancer, it needs to work other drugs to overcome the persistence nature of tumour cells

Food

C-phycocyanin C-PC can be used as a natural blue food colouring[42] This food colourant can only be used for low temperature prepared goods because of its inability to maintaining its blue colouring in high heats unless there is an addition of preservatives or sugars[42][43] The type of sugar is irrelevant, C-PC is stable when there is high sugar content Knowing so, C-PC can be used for numerous types of foods, one of which being syrups C-PC can be used for syrups ranging from green to blue colours It can have different green tints by adding yellow food colourings

References

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  2. ^ Brient L, Lengronne M, Bertrand E, Rolland D, Sipel A, Steinmann D, Baudin I, Legeas M, Le Rouzic B, Bormans M February 2008 "A phycocyanin probe as a tool for monitoring cyanobacteria in freshwater bodies" Journal of Environmental Monitoring 10 2: 248–55 doi:101039/b714238b PMID 18246219 
  3. ^ Wang XQ, Li LN, Chang WR, Zhang JP, Gui LL, Guo BJ, Liang DC June 2001 "Structure of C-phycocyanin from Spirulina platensis at 22 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes" Acta Crystallographica Section D 57 Pt 6: 784–92 doi:101107/S0907444901004528 PMID 11375497 
  4. ^ Adir N, Vainer R, Lerner N December 2002 "Refined structure of c-phycocyanin from the cyanobacterium Synechococcus vulcanus at 16 A: insights into the role of solvent molecules in thermal stability and co-factor structure" Biochimica et Biophysica Acta 1556 2-3: 168–74 PMID 12460674 
  5. ^ a b c d e f Ong LJ, Glazer AN May 1987 "R-phycocyanin II, a new phycocyanin occurring in marine Synechococcus species Identification of the terminal energy acceptor bilin in phycocyanins" The Journal of Biological Chemistry 262 13: 6323–7 PMID 3571260 
  6. ^ "Text Search for: phycocyanin" RCSB PDB Retrieved 13 March 2018 
  7. ^ a b "C - PC C - Phycocyanin" AnaSpec 
  8. ^ a b Pizarro SA, Sauer K May 2001 "Spectroscopic study of the light-harvesting protein C-phycocyanin associated with colorless linker peptides" Photochemistry and Photobiology 73 5: 556–63 PMID 11367580 
  9. ^ Glazer AN, Fang S, Brown DM August 1973 "Spectroscopic properties of C-phycocyanin and of its alpha and beta subunits" The Journal of Biological Chemistry 248 16: 5679–85 PMID 4198883 
  10. ^ Stanier RY, Kunisawa R, Mandel M, Cohen-Bazire G June 1971 "Purification and properties of unicellular blue-green algae order Chroococcales" Bacteriological Reviews 35 2: 171–205 PMC 378380  PMID 4998365 
  11. ^ a b Buchweitz M 2016 "Natural Solutions for Blue Colors in Food" In Carle R, Schweiggert RM Handbook on Natural Pigments in Food and Beverages pp 355–384 doi:101016/b978-0-08-100371-800017-8 ISBN 978-0-08-100371-8 
  12. ^ a b Woźniak M, Bradtke KM, Darecki M, Krężel A March 2016 "Empirical Model for Phycocyanin Concentration Estimation as an Indicator of Cyanobacterial Bloom in the Optically Complex Coastal Waters of the Baltic Sea" Remote Sensing 8 3: 212 doi:103390/rs8030212 
  13. ^ Kuddus, M, Singh, P, Thomas, G, & Al-Hazimi, A 2013 Recent developments in production and biotechnological applications of C-phycocyanin BioMed research international, 2013
  14. ^ a b c d e f g h i Kuddus M, Singh P, Thomas G, Al-Hazimi A 2013 "Recent developments in production and biotechnological applications of C-phycocyanin" BioMed Research International 2013: 742859 doi:101155/2013/742859 PMC 3770014  PMID 24063013 
  15. ^ Marquez FJ, Sasaki K, Kakizono T, Nishio N, Nagai S "Growth characteristics of Spirulina platensis in mixotrophic and heterotrophic conditions" Journal of Fermentation and Bioengineering 76 5: 408–410 doi:101016/0922-338x9390034-6 
  16. ^ Ortiz-Álvarez R, de Los Ríos A, Fernández-Mendoza F, Torralba-Burrial A, Pérez-Ortega S 2015-07-16 "Ecological Specialization of Two Photobiont-Specific Maritime Cyanolichen Species of the Genus Lichina" PLOS One 10 7: e0132718 doi:101371/journalpone0132718 PMID 26181436 
  17. ^ Liu J, Zhang X, Sui Z, Zhang X, Mao Y March 2005 "Cloning and characterization of c-phycocyanin operon from the cyanobacterium Arthrospira platensis FACHB341" Journal of Applied Phycology 17 2: 181–185 doi:101007/s10811-005-6418-2 
  18. ^ Guan X, Qin S, Su Z, Zhao F, Ge B, Li F, Tang X July 2007 "Combinational biosynthesis of a fluorescent cyanobacterial holo-alpha-phycocyanin in Escherichia coli by using one expression vector" Applied Biochemistry and Biotechnology 142 1: 52–9 PMID 18025568 
  19. ^ Ohta N, Matsuzaki M, Misumi O, Miyagishima SY, Nozaki H, Tanaka K, Shin-I T, Kohara Y, Kuroiwa T April 2003 "Complete sequence and analysis of the plastid genome of the unicellular red alga Cyanidioschyzon merolae" DNA Research 10 2: 67–77 PMID 12755171 
  20. ^ Tooley AJ, Cai YA, Glazer AN September 2001 "Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-alpha subunit in a heterologous host" Proceedings of the National Academy of Sciences of the United States of America 98 19: 10560–5 doi:101073/pnas181340998 PMC 58505  PMID 11553806 
  21. ^ Eriksen NT August 2008 "Production of phycocyanin--a pigment with applications in biology, biotechnology, foods and medicine" Applied Microbiology and Biotechnology 80 1: 1–14 doi:101007/s00253-008-1542-y PMID 18563408 
  22. ^ Guo N, Zhang X, Lu Y, Song X March 2007 "Analysis on the factors affecting start-up intensity in the upstream sequence of phycocyanin beta subunit gene from Arthrospira platensis by site-directed mutagenesis" Biotechnology Letters 29 3: 459–64 doi:101007/s10529-006-9266-5 PMID 17242853 
  23. ^ Lu Y, Zhang X 15 April 2005 "The upstream sequence of the phycocyanin β subunit gene from Arthrospira platensis regulates expression of gfp gene in response to light intensity" Electronic Journal of Biotechnology 8 1 doi:102225/vol8-issue1-fulltext-9 
  24. ^ Sloth JK, Wiebe MG, Eriksen NT January 2006 "Accumulation of phycocyanin in heterotrophic and mixotrophic cultures of the acidophilic red alga Galdieria sulphuraria" Enzyme and Microbial Technology 38 1-2: 168–175 doi:101016/jenzmictec200505010 
  25. ^ Chaneva G, Furnadzhieva S, Minkova K, Lukavsky J 23 March 2007 "Effect of light and temperature on the cyanobacterium Arthronema africanum - a prospective phycobiliprotein-producing strain" Journal of Applied Phycology 19 5: 537–544 doi:101007/s10811-007-9167-6 
  26. ^ Venugopal V, Prasanna R, Sood A, Jaiswal P, Kaushik BD 2006 "Stimulation of pigment accumulation in Anabaena azollae strains: effect of light intensity and sugars" Folia Microbiologica 51 1: 50–6 PMID 16821712 
  27. ^ Narayan MS, Manoj GP, Vatchravelu K, Bhagyalakshmi N, Mahadevaswamy M November 2005 "Utilization of glycerol as carbon source on the growth, pigment and lipid production in Spirulina platensis" International Journal of Food Sciences and Nutrition 56 7: 521–8 doi:101080/09637480500410085 PMID 16503562 
  28. ^ Troxler RF, Ehrhardt MM, Brown-Mason AS, Offner GD December 1981 "Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium II Complete amino acid sequence of the beta subunit" The Journal of Biological Chemistry 256 23: 12176–84 PMID 7028751 
  29. ^ "Phycocyanin from Algae and Applications" Oilgae 
  30. ^ a b Romay C, Armesto J, Remirez D, González R, Ledon N, García I January 1998 "Antioxidant and anti-inflammatory properties of C-phycocyanin from blue-green algae" Inflammation Research 47 1: 36–41 doi:101007/s000110050256 PMID 9495584 
  31. ^ Romay C, González R, Ledón N, Remirez D, Rimbau V June 2003 "C-phycocyanin: a biliprotein with antioxidant, anti-inflammatory and neuroprotective effects" Current Protein & Peptide Science 4 3: 207–16 doi:102174/1389203033487216 PMID 12769719 
  32. ^ Romay, C H, Armesto, J, Remirez, D, Gonzalez, R, Ledon, N, & Garcia, I 1998 Antioxidant and anti-inflammatory properties of C-phycocyanin from blue-green algae Inflammation Research, 471, 36-41
  33. ^ a b Romay C, Ledon N, González R Aug 1998 "Further Studies on anti-inflammatory activity of phycocyanin from some animal model of imflammaion" Inflammation Research 47 8: 334–338 doi:101007/s000110050338 PMID 9754867 
  34. ^ Patel, A, Mishra, S, & Ghosh, P K 2006 Antioxidant potential of C-phycocyanin isolated from cyanobacterial species Lyngbya, Phormidium and Spirulina spp
  35. ^ ZHOU, Z P, LIU, L N, CHEN, X L, WANG, J X, Chen, M, ZHANG, Y Z, & ZHOU, B C 2005 FACTORS THAT EFFECT ANTIOXIDANT ACTIVITY OF C‐PHYCOCYANINS FROM SPIRULINA PLATENSIS Journal of food biochemistry, 293, 313-322
  36. ^ a b Min, S K, Park, J S, Luo, L, Kwon, Y S, Lee, H C, Shim, H J, & Shin, H S 2015 Assessment of C-phycocyanin effect on astrocytes-mediated neuroprotection against oxidative brain injury using 2D and 3D astrocyte tissue model Scientific reports, 5, 14418
  37. ^ Liu, Q, Huang, Y, Zhang, R, Cai, T, & Cai, Y 2016 Medical application of Spirulina platensis derived C-phycocyanin Evidence-Based Complementary and Alternative Medicine, 2016
  38. ^ a b Vadiraja, B B, Gaikwad, N W, & Madyastha, K M 1998 Hepatoprotective effect of C-Phycocyanin: protection for carbon tetrachloride andR-+-pulegone-mediated hepatotoxicty in rats Biochemical and Biophysical Research Communications, 2492, 428-431
  39. ^ Basha OM, Hafez RA, El-Ayouty YM, Mahrous KF, Bareedy MH, Salama AM 2008 "C-Phycocyanin inhibits cell proliferation and may induce apoptosis in human HepG2 cells" PDF The Egyptian Journal of Immunology 15 2: 161–7 PMID 20306699 
  40. ^ a b https://wwwhindawicom/journals/ecam/2016/7803846/
  41. ^ Pardhasaradhi BV, Ali AM, Kumari AL, Reddanna P, Khar A November 2003 "Phycocyanin-mediated apoptosis in AK-5 tumor cells involves down-regulation of Bcl-2 and generation of ROS" Molecular Cancer Therapeutics 2 11: 1165–70 PMID 14617790 
  42. ^ a b Martelli G, Folli C, Visai L, Daglia M, Ferrari D January 2014 "Thermal stability improvement of blue colorant C-Phycocyanin from Spirulina platensis for food industry applications" Process Biochemistry 49 1: 154–159 doi:101016/jprocbio201310008 
  43. ^ Chaiklahan R, Chirasuwan N, Bunnag B April 2012 "Stability of phycocyanin extracted from Spirulina sp: Influence of temperature, pH and preservatives" Process Biochemistry 47 4: 659–664 doi:101016/jprocbio201201010 

Further reading

  • Barsanti L 2008 "Oddities and Curiosities in the Algal World" PDF In Evangelista V, Barsanti L, Frassanito AM, Passarelli V, Gualtieri P Algal Toxins: Nature, Occurrence, Effect and Detection NATO Science for Peace and Security Series A: Chemistry and Biology Dordrecht: Springer pp 353–391 doi:101007/978-1-4020-8480-5_17 

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    29.10.2014


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