Purification of phycobiliproteins from Nostoc sp. by aminohexyl–Sepharose chromatography

Tchernov, A.A.; Minkova, Kaledona; Houbavenska, N. B.; Kovacheva, N.

doi:10.1016/s0168-1656(98)00206-5

Cited by 30 publications

(14 citation statements)

References 17 publications

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“…Considering the extraction ratio, we repeated the extraction treatment three times. It should be emphasized this pretreatment method is much simpler than others that use ultrasound or the addition of chemical compounds (lysozyme, rivanol, acetone, Triton X-100 …; Saxena 1988;Tchernov et al 1999).…”

Section: Extractionmentioning

confidence: 99%

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

et al. 2009

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R-phycoerythrin was purified by means of phenylsepharose 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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Section: Extractionmentioning

confidence: 99%

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

et al. 2009

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“…The fluorescence emission maximum was at 650 nm with an excitation wavelength at 620 nm. Because the absorption spectra of the trimeric and monomeric C-PC forms are affected only slightly by the aggregation state of the protein [13], it is not possible to determine the aggregation state of C-PC by these spectra.…”

Section: C-pc Identificationmentioning

confidence: 99%

“…Nevertheless, the use of this biliprotein has been limited by the tedious preparation of large amounts of the purified protein. Conventional methods for purification of phycobiliproteins involve two steps: pretreatment of the sample to liberate the intracellular material, making a crude extract ready for an isolation step in which the phycobiliproteins are separated using conventional processes [12][13][14]. These schemes involve a combination of several techniques, such as centrifugation, precipitation in ammonium sulfate, ion-exchange chromatography, gel-filtration and chromatography on hydroxyapatite [1,5,7,9,[15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Large-scale recovery of C-phycocyanin from Spirulina platensis using expanded bed adsorption chromatography

Niu

Wang

et al. 2007

Journal of Chromatography B

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“…Rivanol was more widely utilized according to previous reports. It was applied to isolate PBP from Porphyridium cruentum [30] and Nostoc sp [31]. CPC with purity of 3.90 and 3.00 from Spirulina (Arthrospira) fusiformis [32] and Arthronema africanum [29], respectively, were purified after fractional precipitation with rivanol.…”

Section: Primary Isolation Of Pbp From P Yezoensismentioning

confidence: 99%

Large scale preparation of phycobiliproteins from <i>Porphyra yezoensis</i> using co-precipitation with ammonium sulfate

Cai¹,

Li²,

Wu³

et al. 2012

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The purpose of this study was to extract phycobiliproteins (PBP) from Porphyra yezoensis using an optimized procedure and further establish a large scale process for protein production. According to our previous experiences on the extraction of PBP, salting out methods, e.g. ammonium sulfate precipitation, worked more efficiently than isoelectric precipitation, differential centrifugation or ultrafiltration. Thus, we chose ammonium sulfate to coprecipitate PBP in crude solution. After four times of precipitation followed by one time of high speed centrifugation, the maximum purity of crude phycoerythrin and phycocyanin reached 1.94 (A 565 /A 280 ) and 0.85 (A 615 /A 280 ), with a yield of 0.50% and 0.37%, respectively. A total of 0.94 mg phycoerythrin and 0.54 mg phycocyanin with purity of more than 3.2 were obtained from 1 g dried P. yezoensis after additional chromatography. We further scaled up the frozen dried P. yezoensis from 20 g to 400 g, with 1295 mg phycoerythrin and 593 mg phycocyanin obtained.

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Purification of phycobiliproteins from Nostoc sp. by aminohexyl–Sepharose chromatography

Cited by 30 publications

References 17 publications

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

Large-scale recovery of C-phycocyanin from Spirulina platensis using expanded bed adsorption chromatography

Large scale preparation of phycobiliproteins from <i>Porphyra yezoensis</i> using co-precipitation with ammonium sulfate

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Purification of phycobiliproteins from Nostoc sp. by aminohexyl–Sepharose chromatography

Cited by 30 publications

References 17 publications

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

Purification of phycoerythrin from Porphyra yezoensis Ueda (Bangiales, Rhodophyta) using expanded bed absorption

Large-scale recovery of C-phycocyanin from Spirulina platensis using expanded bed adsorption chromatography

Large scale preparation of phycobiliproteins from &lt;i&gt;Porphyra yezoensis&lt;/i&gt; using co-precipitation with ammonium sulfate

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Large scale preparation of phycobiliproteins from <i>Porphyra yezoensis</i> using co-precipitation with ammonium sulfate