Thermal and pH Stability of the B-Phycoerythrin from the Red Algae Porphyridium cruentum

González-Ramírez, Emilio J.; Andújar‐Sánchez, Montserrat; Ortiz‐Salmerón, Emilia; Bacarizo, Julio; Cuadri, Celia; Sobczuk, Tania Mazzuca; Ibáñez, María; Cámara-Artigas, A.; Martínez‐Rodríguez, Sergio

doi:10.1007/s11483-014-9331-x

Cited by 49 publications

(31 citation statements)

References 29 publications

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“…This strongly implies that complex formation is a prerequisite for B‐PE pink color and highly fluorescent properties rather than the protonation of the chromophore. Indeed, this is consistent with previous studies whereby a loss of secondary structure was observed by circular dichroism at pH 2 .…”

Section: Resultssupporting

confidence: 93%

“…In addition to enhancing fluorescence, we show the c subunit plays an important role in stabilizing the intact a 6 b 6 c complex, indeed, no a 6 b 6 complex was observed at any pH without the c complex subunit present. Interestingly, previous work by Mart ınez-Rodr ıguez and coworkers showed no notable changes in fluorescence over a pH range of 4-10 from which it was hypothesized that B-PE is stable [13]. Indeed, consistent with their observations, we observed only a very small decrease in fluorescence between pH 4 and pH 8 (Fig.…”

Section: Discussionsupporting

confidence: 91%

“…Upon lowering the pH, B‐PE changes to a purple color (Fig. and ), however, the structural reasons underlying this change are not known. Thus, next, we chose to monitor B‐PE as a function of pH.…”

Section: Resultsmentioning

confidence: 99%

“… demonstrating that the mass spectrometry buffer used (200 m m ammonium acetate) does not affect the fluorescent properties of B‐PE. The excitation wavelengths were chosen based on the three characteristic peaks in the absorbance spectrum of B‐PE at pH 7 . A 1‐cm path length cuvette was used and the temperature maintained at 21 °C throughout.…”

Section: Methodsmentioning

confidence: 92%

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Connecting color with assembly in the fluorescent B‐phycoerythrin protein complex

2017

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Phycoerythrin is the major light-harvesting pigment protein in red algae and is nowadays widely used as a fluorescent probe in biotechnological applications such as flow cytometry and immunofluorescence microscopy. In addition, it has had substantial economic impact due to its potential as a natural food colorant. However, knowledge on the precise molecular composition of phycoerythrin is limited. Here, we use a combination of high-resolution native mass spectrometry (MS) and fluorescence spectroscopy to characterize the assembly properties of the B-phycoerythrin protein complex from Porphyridium cruentum. Our data highlight the stabilizing role of the c subunit in the intact B-phycoerythrin protein complex. In addition, by native MS we monitor B-phycoerythrin (dis)assembly intermediates, providing insight into which species contribute to B-phycoerythrins color and the factors that give B-phycoerythrin its highly fluorescent properties. Together, the data provide significant insights into the structural properties of B-phycoerythrin which is beneficial for its use within the biotechnology industry.

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Section: Resultssupporting

confidence: 93%

Section: Discussionsupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 92%

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Connecting color with assembly in the fluorescent B‐phycoerythrin protein complex

2017

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“…14 (1) chromophore (Munier et al, 2014). According to González-Ramírez et al (2014), changes in the state of protonation on amino acid residues have a large effect on changes in spectral properties of PB. Spectroscopic changes due to low pH may be the result of differences in the state of protonation in the propionate group in the structure of PEB or in the aspartate residues that bind to the group (Camara-Artigas et al, 2012).…”

Section: Pece Stability Of Phmentioning

confidence: 99%

Color Stability of Phycoerythrin Crude Extract (PECE) from Rhodomonas Salina Toward Physicochemical Factors

Marraskuranto

Raharjo

Kasiamdari

et al. 2019

Squalen Bull. Marine Fisheries Postharvest Biotech.

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Rhodomonas salina produces Cr-phycoerythrin545 as its designated phycoerythrin (PE) with an absorption maximum at 545 nm and a shoulder 564 nm. PE has potential to be applied as colorants, pharmaceutical agents, and fluorescent dye tags. The stability of the PE color is influenced by the physicochemical factors of the solution. This study aimed to analyze the color stability of PECE against chemical (ethanol and pH) and physical (light and temperature) factors. PECE was prepared from freeze-dried biomass of R. salina and was extracted in phosphate buffer solution (pH = 6.0) using a freeze-thaw method in -25 oC (2 hours) and 4 oC (24 hours). The resulting extract was concentrated and dried in a freeze-dryer. Analyses were conducted using UV-visible and fluorescence spectrophotometer. PECE showed color stability against light of white fluorescent lamp exposure up to 8 hours, temperature exposure up to 40 oC, ethanol solution up to concentration of 20 % (v/v), and pH range 3.9-8.42. Results from this study can be useful for extraction, purification, and future application of Cr-PE545.

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Analytical Protocols in Phycobiliproteins Analysis

Nikolić

Minić

Mačvanin

et al. 2020

Pigments From Microalgae Handbook

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The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (10 5 to 10 6 ) and excellent fluorescent quantum yield (0.51 up to 0.98).Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their, bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions, identification by proteomics, phycobiliprotein (chromo)peptides and computational studies of structural and dynamic properties.

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Thermal and pH Stability of the B-Phycoerythrin from the Red Algae Porphyridium cruentum

Cited by 49 publications

References 29 publications

Connecting color with assembly in the fluorescent B‐phycoerythrin protein complex

Connecting color with assembly in the fluorescent B‐phycoerythrin protein complex

Color Stability of Phycoerythrin Crude Extract (PECE) from Rhodomonas Salina Toward Physicochemical Factors

Analytical Protocols in Phycobiliproteins Analysis

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