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Guangce Wang - One of the best experts on this subject based on the ideXlab platform.
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purification of Phycoerythrin from porphyra yezoensis ueda bangiales rhodophyta using expanded bed absorption
Journal of Applied Phycology, 2010Co-Authors: Jianfeng Niu, Guangce Wang, Zhangfan Chen, Bai-cheng ZhouAbstract:R-Phycoerythrin was purified by means of phenyl-sepharose expanded bed absorption and DEAE-sepharose ion-exchange chromatography from Porphyra yezoensis, one of the largest and important aquaculture species in China. Final R-Phycoerythrin preparation was characterized by purity ratio above 4 and the homogeneity in native PAGE, respectively. The results of absorption spectrum, fluorescence spectrum and SDS-PAGE were in agreement with previous reports on R-PE. The yield of R-Phycoerythrin was 0.82 mg g(-1) wet leafy gametophyte of P. yezoensis. This method is a high-protein recovery technology while reducing processing time, and is suitable for the large batch production of R-Phycoerythrin, which will enhance the value of P. yezoensis in China, especially the inferior P. yezoensis which can not be used for flake processing.
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method for large scale isolation and purification of r Phycoerythrin from red alga polysiphonia urceolata grev
Protein Expression and Purification, 2006Co-Authors: Jianfeng Niu, Guangce Wang, Chengkui TsengAbstract:R-Phycoerythrin was isolated and purified from a red alga, Polysiphonia urceolata Grev, using Streamline column combined with ion-exchange chromatography or hydroxyapatite chromatography. The purity of R-Phycoerythrin isolated by Streamline column was up to 1.66 and the yield of R-Phycoerythrin could be as high as 0.68 mg/g frozen P. urceolata. All the eluates from Streamline column were divided into two equivalent parts, respectively. One part was pumped into the ion-exchange column loaded with Q-Sepharose and the other was applied to the adsorption column loaded with hydroxyapatite. The purities of R-Phycoerythrin purified using these two methods were both up to 3.26, more than 3.2 the commonly accepted criterion. The yield of purified R-Phycoerythrin from the ion-exchange chromatography was 0.40 mg/g frozen P. urceolata and that from the hydroxyapatite chromatography could reach 0.34 mg/g frozen P. urceolata. The purified protein had three absorption peaks at 498, 535, and 565 nm and displayed a fluorescence maximum at 580 nm, which was consistent with the typical spectrum of R-Phycoerythrin. The purified R-PE was also identified with electrophoresis. Only one single protein band appeared on native-PAGE with silver staining. SDS-PAGE demonstrated the presence of one 20 kDa major subunit, and one low intensity band corresponding to 33 kDa subunit. The results indicate that using the expanded bed adsorption combined with ion-exchange chromatography or hydroxyapatite chromatography, R-Phycoerythrin can be purified from frozen P. urceolata on large scale.
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isolation and purification of Phycoerythrin from red alga garcilaria verrucosa by expanded bed adsorption and ion exchange chromatogaphy
Chromatographia, 2002Co-Authors: Guangce WangAbstract:R-Phycoerythrin was isolated and purified from Gracilaria verrucosa on an expanded-bed adsorption column combined with ion-exchange chromatography, which can effectively solve the problem of blockage of chromatographic columns due to polysaccharides during isolation and purification of phycobiliproteins. 0.1 M (NH4)(2)SO4 proved best to elute R-Phycoerythrin from the expanded-bed column, and desalted 0.1 M (NH4)(2)SO4 eluate was used on an ion-exchange column to purify the R-Phycoerythrin. Using this two-stage chromatography, the purity (OD565/OD280) of the R-Phycoerythrin from G. verrucosa is increased to 4.4, and the yield of purified R-Phycoerythrin can reach 0.141 mg . g(-1) of the frozen alga.
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isolation and purification of Phycoerythrin from red algagracilaria verrucosa by expanded bed adsorption and ion exchange chromatography
Chromatographia, 2002Co-Authors: Guangce WangAbstract:R-Phycoerythrin was isolated and purified from Gracilaria verrucosa on an expanded-bed adsorption column combined with ion-exchange chromatography, which can effectively solve the problem of blockage of chromatographic columns due to polysaccharides during isolation and purification of phycobiliproteins. 0.1 M (NH4)(2)SO4 proved best to elute R-Phycoerythrin from the expanded-bed column, and desalted 0.1 M (NH4)(2)SO4 eluate was used on an ion-exchange column to purify the R-Phycoerythrin. Using this two-stage chromatography, the purity (OD565/OD280) of the R-Phycoerythrin from G. verrucosa is increased to 4.4, and the yield of purified R-Phycoerythrin can reach 0.141 mg . g(-1) of the frozen alga.
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large scale isolation and purification of r Phycoerythrin from red alga palmaria palmata using the expanded bed adsorption method
Journal of Integrative Plant Biology, 2002Co-Authors: Guangce Wang, C. K. TsengAbstract:R-Phycoerythrin, a light-harvesting protein in some marine algae, and can be widely used in medicine, was isolated and purified from a red alga, Palmaria palmata (Lannaeus) Kuntze, using the streamline column (expanded bed adsorption) combined with ion-exchange chromatography. Because the crude extract was applied to the column upwardly, the column would not be blocked by polysaccharides usually very abundant in the extract of marine alga, this kind of blockage could hardly lie overcome in ordinary chromatographic column. After applying the crude extract containing 0.5 mol/L (NH4)(2)SO4, (NH4)(2)SO4 solution of different concentrations (0.2 mol/L, 0.1 mol/L and 0.05 mol/L) was used to elute the column downwardly and the eluates were collected and desalted. The desalted eluates were then applied onto all ion-exchange chromatographic column loaded with Q-sepharose for further purification of the R-Phycoerythrin. Through these two steps, the purity (OD565/OD280) of the R-Phycoerythrin from P. palmata was up to 3.5, more than 3.2, the commonly accepted criterion for purity, and the yield of the purified R-Phycoerythrin could reach 0.122 mg/g of frozen P. palmata, much higher than that of phycobiliproteins purified with the previous methods. The result indicated that the cost of R-Phycoerythrin will drop down with the method reported in this article.
Joel Fleurence - One of the best experts on this subject based on the ideXlab platform.
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physicochemical factors affecting the stability of two pigments r Phycoerythrin of grateloupia turuturu and b Phycoerythrin of porphyridium cruentum
Food Chemistry, 2014Co-Authors: Mathilde Munier, Sebastien Jubeau, Alva Wijaya, Michele Morancais, Justine Dumay, Luc Marchal, Pascal Jaouen, Joel FleurenceAbstract:Abstract Phycoerythrin is a major light-harvesting pigment of red algae, which could be used as a natural dye in foods. The stability of R-Phycoerythrin of Grateloupia turuturu and B-Phycoerythrin of Porphyridium cruentum in relation to different light exposure times, pHs, and temperatures was studied. Regarding the light exposure time, after 48 h, the reduction in concentrations of B-Phycoerythrin and R-Phycoerythrin were 30 ± 2.4% and 70 ± 1%, respectively. Phycoerythrins presented good stability from pH 4 to 10. At pH 2, the reduction in concentration was 90 ± 4% for B-Phycoerythrin and 40 ± 2.5% for R-Phycoerythrin while, at pH 12, the Phycoerythrins were degraded. Phycoerythrins showed good stability toward temperature, up to 40 °C. At 60 °C, the reduction in concentrations of B-Phycoerythrin and R-Phycoerythrin were 50 ± 3.4% and 70 ± 0.18%, respectively. Moreover, the best conditions of storage (−20 °C) were determined.
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optimization of hydrolysis conditions of palmaria palmata to enhance r Phycoerythrin extraction
Bioresource Technology, 2013Co-Authors: Justine Dumay, Michele Morancais, Nathalie Clement, Joel FleurenceAbstract:In this study, response surface methodology was applied to optimize R-Phycoerythrin extraction from the red seaweed Palmaria palmata, using enzymatic digestion. Several algal treatments prior to digestion were first investigated. The extraction yield and the purity index of R-Phycoerythrin, and the recovery of proteins and reducing sugars in the water-soluble fraction were then studied in relation to the hydrolysis time, the temperature and the enzyme/seaweed ratio. Enzymatic digestion appears to be an effective treatment for R-Phycoerythrin extraction. Moreover, using the seaweed roughly cut in its wet form gives the most interesting results in terms of extract quality and economic cost. The R-Phycoerythrin extraction yield is 62 times greater than without enzyme treatment and 16 times greater than without optimization. Enzymatic optimization enhanced the purity index up to 16 times.
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concentration and pre purification with ultrafiltration of a r Phycoerythrin solution extracted from macro algae grateloupia turuturu process definition and up scaling
Separation and Purification Technology, 2009Co-Authors: Claire Denis, Joel Fleurence, Anthony Masse, Pascal JaouenAbstract:abstract Grateloupia turuturu , an invasive red macro-alga, represents an unexploited important biomass. A poten-tial use of this seaweed is the production of valuable molecules, such as R-Phycoerythrin. Nevertheless,after R-Phycoerythrin extraction, protein extract has to be concentrated and pre-purified, which is gen-erally expensive and requires many stages. The present study deals with the feasibility to implement asingle stage of ultrafiltration for this purpose.A membrane screening was first realized at a lab-scale (Amicon stirred cell) to determine a suitablemembrane molecular weight cut-off and a material allowing an optimal concentration and pre-purification of R-Phycoerythrin contained in a hydrosoluble extract. The best adapted membrane turnedouttobeapolyethersulfone30kDaone.Anup-scalingmethodologywasthenrealizedonaPCIMicrolab40pilot plant equipped with an industrial type polyethersulfone 25–30kDa membrane. The results showthat R-Phycoerythrin was concentrated without denaturation and accumulation of undesired molecules.Ultrafiltration up to a volume reduction factor of 5 was effective for R-Phycoerythrin concentration andpre-purification: 100% of R-Phycoerythrin was recovered, 32.9% of other proteins and 64.6% of sugarspassed through membrane. Based on these results, a techno-economic study was investigated on anultrafiltration unit at an industrial scale.© 2009 Elsevier B.V. All rights reserved.
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one step purification of r Phycoerythrin from the red macroalga palmaria palmata using preparative polyacrylamide gel electrophoresis
Journal of Chromatography B: Biomedical Sciences and Applications, 2000Co-Authors: A V Gallandirmouli, Michel Lucon, L Pons, N T Mrabet, Joel FleurenceAbstract:Abstract Phycoerythrin is a major light-harvesting pigment of red algae and cyanobacteria widely used as a fluorescent probe. In this study, Phycoerythrin of the red macroalga Palmaria palmata was extracted by grinding the algal sample in liquid nitrogen, homogenisation in phosphate buffer and centrifugation. Phycoerythrin was then purified from this crude extract using preparative polyacrylamide gel electrophoresis (PAGE) with a continuous elution system and detected by its pink colour and fluorescence. The pigment presented a typical spectrum of R-Phycoerythrin, with three absorbance maxima at 499, 545 and 565 nm, and displayed a fluorescence maximum at 578 nm. The absorbance ratio A 565 / A 280 , a criterion for purity, was 3.2. A single protein of relative molecular mass 240 000 was detected on native-PAGE with silver staining. Sodium dodecyl sulphate–PAGE demonstrated the presence of two major subunits with M r 20 000 and 21 000, respectively, and a very minor subunit of M r 30 000. These observations are consistent with the (αβ) 6 γ subunit composition characteristic of R-Phycoerythrin. Phycoerythrin of Palmaria palmata was determined to be present in larger amounts in autumn and showed a good stability up to 60°C and between pH 3.5 and 9.5. In conclusion, Phycoerythrin of Palmaria palmata was purified in a single-step using preparative PAGE. Obtaining pure R-Phycoerythrin of Palmaria palmata will allow one to evaluate its fluorescence properties for future applications in biochemical techniques.
Datta Madamwar - One of the best experts on this subject based on the ideXlab platform.
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Crystal structure analysis of C-Phycoerythrin from marine cyanobacterium Phormidium sp. A09DM
Photosynthesis Research, 2016Co-Authors: Vinay Kumar, Ravi R Sonani, Mahima Sharma, Gagan D. Gupta, Datta MadamwarAbstract:The role of unique sequence features of C-Phycoerythrin, isolated from Phormidium sp. A09DM , has been investigated by crystallographic studies. Two conserved indels (i.e. inserts or deletions) are found in the β-subunit of Phormidium Phycoerythrin that are distinctive characteristics of large number of cyanobacterial sequences. The identified signatures are a two-residue deletion from position 21 and a nine-residue insertion at position 146. Crystals of Phormidium Phycoerythrin were obtained at pH values of 5 and 8.5, and structures have been resolved to high precision at 1.95 and 2.1 Å resolution, respectively. In both the structures, heterodimers of α- and β- subunits assemble as hexamers. The 7-residue insertion at position 146 significantly reduces solvent exposure of π-conjugated A–C rings of a phycoerythrobilin (PEB) chromophore, and can influence energy absorption and energy transfer characteristics. The structural analyses (with 12-fold redundancy) suggest that protein micro-environment alone dictates the conformation of bound chromophores. The low- and high-energy absorbing chromophores are identified based on A–B ring coplanarity. The spatial distribution of these is found to be similar to that observed in R-Phycoerythrin, suggesting the direction of energy transfer from outer-surface of hexamer to inner-hollow cavity in the Phormidium protein. The crystal structures also reveal that a commonly observed Hydrogen-bonding network in phycobiliproteins, involving chromophore bound to α-subunit and amino acid at position 73 of β-subunit, may not be essential for structural and functional integrity of C-Phycoerythrin orthologs. In solution, the protein displays slight red shift and decrease in fluorescence emission at acidic pH. The mechanism for which may be static and correlates with the proximity of +ve electric field of Arg148 to the C-ring of a PEB chromophore.
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concurrent purification and antioxidant activity of phycobiliproteins from lyngbya sp a09dm an antioxidant and anti aging potential of Phycoerythrin in caenorhabditis elegans
Process Biochemistry, 2014Co-Authors: Ravi R Sonani, Niraj Kumar Singh, Jitendra Kumar, Dixita Thakar, Datta MadamwarAbstract:Abstract The present study probes into the purification of phycobiliproteins, and characterization of their in vitro anti-oxidant activity. Moreover, the study also demonstrates the use of antioxidant virtue of Phycoerythrin in moderating the phenomenon of aging in Caenorhabditis elegans. Phycoerythrin, phycocyanin and allophycocyanin were purified successfully from Lyngbya sp. A09DM by ammonium sulfate fractionation appended with Triton X-100 intercession. The success of protocol was examined by a series of biochemical characterization like SDS-PAGE, native-PAGE, UV–visible spectroscopy and fluorescence spectroscopy ensuring purity, integrity and functionality of purified Phycoerythrin, phycocyanin and allophycocyanin. Purified phycobiliproteins were evaluated for antioxidant and metal ion chelating activity by various in vitro antioxidant assay systems. Results showed significant and dose-dependent antioxidant as well as metal chelating potential of all phycobiliproteins in decreasing order of Phycoerythrin > phycocyanin > allophycocyanin. Expansion in lifespan and improvement in pharyngeal pumping of C. elegans were noticed upon pre-treatment with Phycoerythrin (100 μg ml−1). Moreover, Phycoerythrin mediated increase in worm survival under oxidative stress revealed that the life expansion effect of Phycoerythrin on nematode is in part by an action of its antioxidant virtue. These results collectively added up evidence in favor of the ‘free-radical theory of aging’. The present report, for the first time, describes antioxidant potential of Phycoerythrin and its use in extending life-span of C. elegans.
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characterization of an intact Phycoerythrin and its cleaved 14 kda functional subunit from marine cyanobacterium phormidium sp a27dm
Process Biochemistry, 2011Co-Authors: Asha Parmar, Niraj Kumar Singh, Avani Kaushal, Datta MadamwarAbstract:Abstract In this study, we describe a series of experiments presenting the biochemical evidence for the cleavage of an intact Phycoerythrin (α and β subunits) to Phycoerythrin with only fragmented α-subunit, which is also functional, in Phormidium sp. A27DM. Culture, whether grown in different conditions (static or sparging) or in medium with different pH, produced truncated Phycoerythrin. This indicated that the growth conditions or pH of medium did not lead to cleavage of Phycoerythrin. Culture when grown in the medium lacking NaNO 3 started producing truncated Phycoerythrin after 9 days of growth only, thus proving that nitrogen depletion was playing a role in Phycoerythrin cleavage. In vivo and in vitro experiments with different proteases also resulted in production of truncated Phycoerythrin. And on the addition of different protease inhibitors intact Phycoerythrin formation was taking place even after 60 days of growth, thus indicating the possible role of proteases in Phycoerythrin cleavage. Moreover, purified intact PE when stored at 4 °C also gets cleaved to 14 kDa fragment. However, when glacial acetic acid was added to Phycoerythrin no cleavage was observed even after 4 months of storage. The events indicate that production of truncated PE is meant for continuing the absorption of light under stress conditions.
David M. Kehoe - One of the best experts on this subject based on the ideXlab platform.
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Self-regulating genomic island encoding tandem regulators confers chromatic acclimation to marine Synechococcus
Proceedings of the National Academy of Sciences of the United States of America, 2016Co-Authors: Joseph E. Sanfilippo, Jonathan A. Karty, Wendy M. Schluchter, Laurence Garczarek, Frédéric Partensky, Animesh Shukla, Adam A. Nguyen, David M. KehoeAbstract:The evolutionary success of marine Synechococcus, the second-most abundant phototrophic group in the marine environment, is partly attributable to this group’s ability to use the entire visible spectrum of light for photosynthesis. This group possesses a remarkable diversity of light-harvesting pigments, and most of the group’s members are orange and pink because of their use of phycourobilin and phycoerythrobilin chromophores, which are attached to antennae proteins called Phycoerythrins. Many strains can alter Phycoerythrin chromophore ratios to optimize photon capture in changing blue–green environments using type IV chromatic acclimation (CA4). Although CA4 is common in most marine Synechococcus lineages, the regulation of this process remains unexplored. Here, we show that a widely distributed genomic island encoding tandem master regulators named FciA (for type four chromatic acclimation island) and FciB plays a central role in controlling CA4. FciA and FciB have diametric effects on CA4. Interruption of fciA causes a constitutive green light phenotype, and interruption of fciB causes a constitutive blue light phenotype. These proteins regulate all of the molecular responses occurring during CA4, and the proteins’ activity is apparently regulated posttranscriptionally, although their cellular ratio appears to be critical for establishing the set point for the blue–green switch in ecologically relevant light environments. Surprisingly, FciA and FciB coregulate only three genes within the Synechococcus genome, all located within the same genomic island as fciA and fciB. These findings, along with the widespread distribution of strains possessing this island, suggest that horizontal transfer of a small, self-regulating DNA region has conferred CA4 capability to marine Synechococcus throughout many oceanic areas.
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Phycoerythrin-specific bilin lyase-isomerase controls blue-green chromatic acclimation in marine Synechococcus.
Proceedings of the National Academy of Sciences of the United States of America, 2012Co-Authors: Animesh Shukla, Jonathan A. Karty, Wendy M. Schluchter, Laurence Garczarek, Frédéric Partensky, Avijit Biswas, Nicolas Blot, Loubna A Hammad, Andrian Gutu, David M. KehoeAbstract:The marine cyanobacterium Synechococcus is the second most abundant phytoplanktonic organism in the world's oceans. The ubiquity of this genus is in large part due to its use of a diverse set of photosynthetic light-harvesting pigments called phycobiliproteins, which allow it to efficiently exploit a wide range of light colors. Here we uncover a pivotal molecular mechanism underpinning a widespread response among marine Synechococcus cells known as "type IV chromatic acclimation" (CA4). During this process, the pigmentation of the two main phycobiliproteins of this organism, Phycoerythrins I and II, is reversibly modified to match changes in the ambient light color so as to maximize photon capture for photosynthesis. CA4 involves the replacement of three molecules of the green light-absorbing chromophore phycoerythrobilin with an equivalent number of the blue light-absorbing chromophore phycourobilin when cells are shifted from green to blue light, and the reverse after a shift from blue to green light. We have identified and characterized MpeZ, an enzyme critical for CA4 in marine Synechococcus. MpeZ attaches phycoerythrobilin to cysteine-83 of the α-subunit of Phycoerythrin II and isomerizes it to phycourobilin. mpeZ RNA is six times more abundant in blue light, suggesting that its proper regulation is critical for CA4. Furthermore, mpeZ mutants fail to normally acclimate in blue light. These findings provide insights into the molecular mechanisms controlling an ecologically important photosynthetic process and identify a unique class of Phycoerythrin lyase/isomerases, which will further expand the already widespread use of Phycoerythrin in biotechnology and cell biology applications.
Camille Loupiac - One of the best experts on this subject based on the ideXlab platform.
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Effect of high hydrostatic pressure on the structure of the soluble protein fraction in Porphyridium cruentum extracts
Innovative Food Science & Emerging Technologies, 2019Co-Authors: Thierry Tran, Céline Lafarge, Rémi Pradelles, Jean-marie Perrier-cornet, Nathalie Cayot, Camille LoupiacAbstract:High hydrostatic pressure (HHP) treatments are trending as “green” stabilization and extraction process. The extraction of B-Phycoerythrin from microalgae is getting more and more interest due to its numerous potentialities in foods, cosmetics and medicine. Thus, the effects of high pressure on the structural characteristics of B-Phycoerythrin extracted from Porphyridium cruentum are explored in this paper. Spectrophotometric methods allowed to measure B-Phycoerythrin content (UV–visible) and gave an indication on the protein structure (fluorescence). Micro-DSC analysis and electrophoresis complemented this structural investigation for all the protein fractions of P. cruentum extracts. Applying high hydrostatic pressure treatments up to 300 MPa during 5 min had no significant effect on B-Phycoerythrin content and structure in P. cruentum extracts. Nevertheless, conformational changes of the protein are suggested by fluorescence yield decrease at 400 MPa, and protein aggregation of B-Phycoerythrin, observed by Micro-DSC and electrophoresis, occurred at 500 MPa. Industrial relevance The HHP process is an emerging technology for the microbiological stability of various food matrices, including the proteins of microalgae as natural colorant. The target pressure to stabilize is around 400 MPa. High hydrostatic pressure can be used on P. cruentum extracts up to 300 MPa without any change in protein structure, as the threshold of protein aggregation is observed at 400 MPa. The observed changes of the proteins structure after applying HHP above 400 MPa can have a strong impact at macroscopic scale on the food matrices: increase of turbidity, change of texture, stability of emulsion.
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ex situ and in situ investigation of protein exopolysaccharide complex in porphyridium cruentum biomass resuspension
Algal Research-Biomass Biofuels and Bioproducts, 2019Co-Authors: Thierry Tran, Céline Lafarge, Rémi Pradelles, Nathalie Cayot, Pascale Winckler, Camille LoupiacAbstract:Abstract During the extraction processes of B-Phycoerythrin from P. cruentum, the possibility of the occurrence of extraction-inhibiting B-Phycoerythrin/exopolysaccharide (EPS) complexes was highlighted. The use of confocal laser scanning microscopy allowed the observation of the cells including their sheath and their chloroplast, the bound EPS matrix, and extracellular vesicles involving phycobiliproteins and EPS in P. cruentum biomass resuspensions. The observations were performed using autofluorescence and fluorescence marking. pH variations showed more impact than ionic strength increase induced by NaCl addition on the B-Phycoerythrin content and the organization of vesicles. Namely, agglomeration of the vesicles could be observed at pH 8.5 without NaCl addition. With addition of 1 M NaCl, this phenomenon was prevented but the vesicles were not visibly dissociated for any pH value. These results point towards a precipitate rather than a coacervate, which are expected to have narrow stability conditions regarding pH and ionic strength. In an attempt to dissolve or break the vesicles and the extracellular matrix, successive macerations in water and use of high pressure homogenizer process in one-step or two-step treatments were applied to the resuspensions. The successive macerations could free the cells and the vesicles from the extracellular matrix, whereas the homogenizer treatment disrupted the extracellular matrix, the vesicle and a part of the cells. In our case, only the successive macerations showed a positive extraction since the high pressure treatment caused unwanted denaturation. It is concluded that more experiments in model conditions could help understand the nature of the interactions between phycobiliproteins and EPS leading to the formation of the vesicles. Porphyridium cruentum, confocal fluorescence microscopy, complexation, B-Phycoerythrin, exopolysaccharide.
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Effect of high hydrostatic pressure on extraction of B-Phycoerythrin from Porphyridium cruentum: Use of confocal microscopy and image processing
Algal Research - Biomass Biofuels and Bioproducts, 2019Co-Authors: Thierry Tran, Céline Lafarge, Rémi Pradelles, Jean-marie Perrier-cornet, Camille Loupiac, Emmanuel Denimal, Ludovic Journaux, John Aldo Lee, Pascale Winckler, Nathalie CayotAbstract:The aim of the study was to extract B-Phycoerythrin from Porphyridium cruentum while preserving its structure. The high hydrostatic pressure treatments were chosen as extraction technology. Different methods have been used to observe the effects of the treatment: spectrophotometry and confocal laser scanning microscopy followed by image processing analysis. Image processing led to the generation of masks used for the identification of three clusters: intra, extra and intercellular. All methods showed that high hydrostatic pressure treatments between 50 and 500 MPa failed to extract B-Phycoerythrin from Porphyridium cruentum cells. The fluorescence emission was negatively impacted by high hydrostatic pressure treatment from 400 MPa for the extracellular and intercellular cluster and from 500 MPa for the intercellular cluster. These results suggest that high pressure treatments could induce the denaturation of B-Phycoerythrin in all clusters but with different intensities depending on the cluster.