One-step chromatography method for efficient separation and purification of R-phycoerythrin from Polysiphonia urceolata

Liu, Luning; Chen, Xiu-Lan; Zhang, Xiying; Zhang, Yu-Zhong; Zhou, Biao

doi:10.1016/j.jbiotec.2004.09.017

Cited by 119 publications

(62 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phycoerythrin displays a good stability to pH variations between pH 3.5 and 9.5. In the fluorescence spectra, the emission maxima decreased about 10% along with the pH value fell from 7.0 to 4.4; at the same time, the emission wavelength red-shifted a little from 580 to 581 nm (Liu, Chen et al, 2005;Liu, Su et al, 2009;Sun & Wang, 2000;Sun et al, 2009). Phycoerythrin was found to be sensitive to heat and light in aqueous solution; PE is insoluble in acidic solution (pH 3.0) and is highly soluble and stable at pH 7.0.…”

Section: Phycobiliproteins Extractionmentioning

confidence: 95%

“…Phycoerythrin was found to be sensitive to heat and light in aqueous solution; PE is insoluble in acidic solution (pH 3.0) and is highly soluble and stable at pH 7.0. When phycobilisomes are exposed to dilute buffers with pH 6-7, the phycobilisomes dissociate into their components, and individual biliproteins can be identified and purified (Lawrenz & Fedewa, 2011;Liu, Chen et al, 2005;MacColl, 2004;Mishra et al, 2010;Sampath-Wiley & Neefus, 2007).…”

Section: Phycobiliproteins Extractionmentioning

confidence: 99%

“…They exhibit a large Stokes shift which is very important (Liu, Chen et al, 2005;Niu et al, 2006;Sun et al, 2003).…”

Section: Spectrofluorimetrymentioning

confidence: 99%

“…The PEs appear bright pink color, PCs are dark cobalt blue, and APCs are brighter aqua blue. The absorption maxima are 540-570, 610-620, and 650-655 nm for PE, PC, and APC, respectively (Ba´saca-Loya et al, 2009;Isailovic, Sultana, Phillips, & Yeung, 2006;Lawrenz & Fedewa, 2011;Liu, Chen, Zhang, Zhang, & Zhou, 2005;Liu, Su et al, 2009;Mishra et al, 2010;Niu, Wang, & Tseng, 2006;Sun, Wang, Chen, & Gong, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…One of the most frequently cited phycobilin quantification techniques utilize the spectral properties of crude aqueous extracts to estimate the pigments content of sample tissues. The samples are ground, extracted in phosphate buffer, centrifuged, and the absorbance values or fluorescence of the supernatant corresponding to peaks and troughs of phycobiliproteins are recorded (Ba´saca-Loya et al, 2009;Denis et al, 2010;Liu, Chen et al, 2005;Sampath-Wiley & Neefus, 2007;Sun & Wang, 2000;Xu & Gao, 2008). This paper describes a constant-wavelength synchronous scan spectrofluorimetric method for the individual determination of the three phycobiliproteins very abundant in red algae: PE, PC, and APC.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Determination of phycobiliproteins by constant-wavelength synchronous spectrofluorimetry method in red algae

Yusty

Adán

López-Hernández

2013

CyTA - Journal of Food

View full text Add to dashboard Cite

Phycobiliproteins are pigment-protein complexes, brilliant-colored and water soluble, existing in cyanobacteria and red algae. They have a great interest in food technology, food supplements, and pharmaceutical applications. Therefore it is important to have a fast, easy, and reliable method to determine the content of phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (APC) in red algae. The samples are ground, extracted in phosphate buffer (pH 6.8), centrifuged, and the fluorescence scan of the supernatant is recorded. Optimum excitation-emission wavelength intervals (Dl) for synchronous spectrofluorimetric analysis of the three phycobiliproteins were 10 nm for PE (LD ¼ 10.9 6 10 73 mg/l) and APC (LD ¼ 0.5 mg/l) and 40 nm for PC (LD ¼ 0.77 mg/l). Algae analyzed contain PC and PE.

show abstract

Section: Phycobiliproteins Extractionmentioning

confidence: 95%

Section: Phycobiliproteins Extractionmentioning

confidence: 99%

“…They exhibit a large Stokes shift which is very important (Liu, Chen et al, 2005;Niu et al, 2006;Sun et al, 2003).…”

Section: Spectrofluorimetrymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Determination of phycobiliproteins by constant-wavelength synchronous spectrofluorimetry method in red algae

Yusty

Adán

López-Hernández

2013

CyTA - Journal of Food

View full text Add to dashboard Cite

show abstract

Purification of β‐Galactosidase by Ion Exchange Chromatography: Elution Optimization Using an Experimental Design

2012

View full text Add to dashboard Cite

Purification of b-Galactosidase by Ion Exchange Chromatography: Elution Optimization Using an Experimental Designb-Galactosidase is an enzyme industrially used to hydrolyze milk lactose, generating dairy products destined for people intolerant to this sugar. Its importance is due to its galactosiltransferase activity. The effects of elution pH and salt gradient volume were evaluated for purification of b-galactosidase by ion exchange chromatography using an experimental design and response surface techniques. The best conditions for purification of b-galactosidase were pH 5.5 with an elution volume of 62.8 mL, obtaining a yield of 85.5 % and a 12-fold increase in the purification factor in a one-step chromatography process. Purification of b-galactosidase by application of a single stage of ion exchange and evaluation of the important process parameters using an experimental design provided good results in the recovery and purification factor that could subsequently be scaled up. Ion exchange chromatography 911where A is the activity [U mL -1 ], P is the total protein concentration (mg mL -1 ), and V is the volume (mL).

show abstract

Expanded and fixed bed ion exchange chromatography for the recovery of C‐phycocyanin in a single step by using lysed cells

et al. 2014

View full text Add to dashboard Cite

C‐phycocyanin, a natural blue dye, stands out today because it has antioxidant, anti‐inflammatory, and anti‐tumor properties, and it can be extracted from cyanobacteria, such as the genus Spirulina. A process that has received attention is the adsorption of proteins in the presence of biomass by fluidized bed, particularly an expanded bed. Therefore, this study aimed at purifying C‐phycocyanin by ion exchange chromatography in expanded bed in the presence of biomass with two different resins (Streamline Q XL and Streamline DEAE) and comparing the purification process of C‐phycocyanin by applying the fixed bed ion exchange chromatography. The expanded bed purification carried out with the support of Streamline Q XL was considered more promising than with Streamline DEAE since the former had higher C‐phycocyanin recovery than the latter. The fraction C‐phycocyanin in the expanded bed mode with Streamline Q XL had average purity of 1.6, concentration of 2.4 mg mL−1, and recovery process of 79 %. Moreover, by comparison with the fixed bed, the recovery of C‐phycocyanin was higher in the expanded mode, even though both purity levels were similar. It has been shown that such crude feedstocks can be applied to the bed without prior clarification steps. As a result, the single‐step recovery process (clarification, capture, and purification) can be established, thus eliminating the centrifugation step, saving energy, and reducing the cost of the process.

show abstract

One-step chromatography method for efficient separation and purification of R-phycoerythrin from Polysiphonia urceolata

Cited by 119 publications

References 27 publications

Determination of phycobiliproteins by constant-wavelength synchronous spectrofluorimetry method in red algae

Determination of phycobiliproteins by constant-wavelength synchronous spectrofluorimetry method in red algae

Purification of β‐Galactosidase by Ion Exchange Chromatography: Elution Optimization Using an Experimental Design

Expanded and fixed bed ion exchange chromatography for the recovery of C‐phycocyanin in a single step by using lysed cells

Contact Info

Product

Resources

About