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Datta Madamwar - One of the best experts on this subject based on the ideXlab platform.

  • optimization of medium components for increased production of c Phycocyanin from phormidium ceylanicum and its purification by single step process
    Bioresource Technology, 2009
    Co-Authors: Niraj Kumar Singh, Asha Parmar, Datta Madamwar
    Abstract:

    Phycocyanin is a major protein produced by cyanobacteria, but very few Phycocyanin-producing strains have been reported. In the present study, response surface methodology (RSM) involving a central composite design for four factors was successfully employed to optimize medium components for increased production of Phycocyanin from Phormidium ceylanicum. The production of Phycocyanin and interactions between sodium nitrate, calcium chloride, trace metal mix and citric acid stock were investigated and modeled. Under optimized condition P. ceylanicum was able to give 2.3-fold increase in Phycocyanin production in comparison to commonly used BG 11 medium in 32 days. We have demonstrated the extraction, purification and characterization of C-Phycocyanin using novel method based on filtration and single step chromatography. The protein was extracted by repeated freeze-thaw cycles and the crude extract was filtered and concentrated in stirred ultrafiltration cell (UFC). The UFC concentrate was then subjected to a single ion exchange chromatographic step. A purity ratio of 4.15 was achieved from a starting value of 1.05. The recovery efficiency of C-Phycocyanin from crude extract was 63.50%. The purity was checked by electrophoresis and UV-Vis spectroscopy.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin – a major phycobiliprotein constitutively produced by many cyanobacteria hold several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (λmax) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported α and β subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted florescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (αβ)3 subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Phycocyanin--a major phycobiliprotein constitutively produced by many cyanobacteria--holds several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (lambda(max)) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported alpha and beta subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted fluorescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (alphabeta)(3) subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • extraction purification and characterization of Phycocyanin from oscillatoria quadripunctulata isolated from the rocky shores of bet dwarka gujarat india
    Process Biochemistry, 2006
    Co-Authors: Badrish Soni, Beena Kalavadia, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin is a major phycobiliprotein produced by cyanobacteria, but only few strains for its efficient purification have been reported until now. In the present study, we discussed the extraction, purification and characterization of C-Phycocyanin from a novel isolate Oscillatoria quadripunctulata . The Phycocyanin was extracted by repeated freeze–thaw cycles and purified by a three-step process: ammonium sulfate fractionation, Sephadex G-150 size exclusion chromatography and DEAE cellulose ion exchange chromatography. Purified Phycocyanin showed absorbance maxima at 620 nm. A purity ratio ( R ) of 3.31 was achieved. The Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin ratio were 4.90 and 3.92, respectively. The recovery efficiency of C-Phycocyanin from crude extract was above 68%. Twenty milligram pure Phycocyanin was obtained from 10 g of dried cell mass. The purified protein showed p I of 5.0. The purity was checked by gel electrophoresis and UV-vis spectroscopy. High performance liquid chromatography (HPLC) determined the molecular weight of intact Phycocyanin to be 215 kDa, whereas denaturing gel electrophoresis showed the presence of two bands of 19 and 20 kDa molecular mass, indicating the characteristic (αβ) 6 subunit assembly of Phycocyanin. Zinc-assisted fluorescence enhancement further confirmed that both subunits are bilin-linked polypeptides.

Badrish Soni - One of the best experts on this subject based on the ideXlab platform.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Phycocyanin--a major phycobiliprotein constitutively produced by many cyanobacteria--holds several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (lambda(max)) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported alpha and beta subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted fluorescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (alphabeta)(3) subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin – a major phycobiliprotein constitutively produced by many cyanobacteria hold several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (λmax) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported α and β subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted florescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (αβ)3 subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • extraction purification and characterization of Phycocyanin from oscillatoria quadripunctulata isolated from the rocky shores of bet dwarka gujarat india
    Process Biochemistry, 2006
    Co-Authors: Badrish Soni, Beena Kalavadia, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin is a major phycobiliprotein produced by cyanobacteria, but only few strains for its efficient purification have been reported until now. In the present study, we discussed the extraction, purification and characterization of C-Phycocyanin from a novel isolate Oscillatoria quadripunctulata . The Phycocyanin was extracted by repeated freeze–thaw cycles and purified by a three-step process: ammonium sulfate fractionation, Sephadex G-150 size exclusion chromatography and DEAE cellulose ion exchange chromatography. Purified Phycocyanin showed absorbance maxima at 620 nm. A purity ratio ( R ) of 3.31 was achieved. The Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin ratio were 4.90 and 3.92, respectively. The recovery efficiency of C-Phycocyanin from crude extract was above 68%. Twenty milligram pure Phycocyanin was obtained from 10 g of dried cell mass. The purified protein showed p I of 5.0. The purity was checked by gel electrophoresis and UV-vis spectroscopy. High performance liquid chromatography (HPLC) determined the molecular weight of intact Phycocyanin to be 215 kDa, whereas denaturing gel electrophoresis showed the presence of two bands of 19 and 20 kDa molecular mass, indicating the characteristic (αβ) 6 subunit assembly of Phycocyanin. Zinc-assisted fluorescence enhancement further confirmed that both subunits are bilin-linked polypeptides.

Ujjval Trivedi - One of the best experts on this subject based on the ideXlab platform.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Phycocyanin--a major phycobiliprotein constitutively produced by many cyanobacteria--holds several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (lambda(max)) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported alpha and beta subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted fluorescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (alphabeta)(3) subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • a novel method of single step hydrophobic interaction chromatography for the purification of Phycocyanin from phormidium fragile and its characterization for antioxidant property
    Bioresource Technology, 2008
    Co-Authors: Badrish Soni, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin – a major phycobiliprotein constitutively produced by many cyanobacteria hold several promising applications in diagnostics, biomedical research, and therapeutics. This paper discusses a novel rapid method for the purification of cyanobacterial Phycocyanin (C-PC) from Phormidium fragile using hydrophobic interaction chromatography. The protein was extracted and concentrated by grinding under liquid nitrogen and ammonium sulfate fractionation. C-PC was purified by single step hydrophobic interaction chromatography. Purified Phycocyanin showed absorbance maximum (λmax) at 624 nm. The criterion of purity (R) achieved was 4.52. Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin purity ratio were 3.85 and 7.49, respectively. The purified protein showed a pI of 5.2 and has two subunits with molecular mass of 19 and 20 kDa each, corresponding to its highly reported α and β subunits. The subunits of Phycocyanin were confirmed by their bilin fluorescence using zinc assisted florescence enhancement technique. Intact C-PC was of 125 kDa as determined by HPLC, suggested the (αβ)3 subunit assembly. Results obtained by this method in terms of purity, recovery, process time, simplicity, and efficacy are much better than previous methodologies. Purified Phycocyanin was further scrutinized for its antioxidant capacity and judged against five non-enzymatic antioxidants by FRAP assay.

  • extraction purification and characterization of Phycocyanin from oscillatoria quadripunctulata isolated from the rocky shores of bet dwarka gujarat india
    Process Biochemistry, 2006
    Co-Authors: Badrish Soni, Beena Kalavadia, Ujjval Trivedi, Datta Madamwar
    Abstract:

    Abstract Phycocyanin is a major phycobiliprotein produced by cyanobacteria, but only few strains for its efficient purification have been reported until now. In the present study, we discussed the extraction, purification and characterization of C-Phycocyanin from a novel isolate Oscillatoria quadripunctulata . The Phycocyanin was extracted by repeated freeze–thaw cycles and purified by a three-step process: ammonium sulfate fractionation, Sephadex G-150 size exclusion chromatography and DEAE cellulose ion exchange chromatography. Purified Phycocyanin showed absorbance maxima at 620 nm. A purity ratio ( R ) of 3.31 was achieved. The Phycocyanin to phycoerythrin and Phycocyanin to alloPhycocyanin ratio were 4.90 and 3.92, respectively. The recovery efficiency of C-Phycocyanin from crude extract was above 68%. Twenty milligram pure Phycocyanin was obtained from 10 g of dried cell mass. The purified protein showed p I of 5.0. The purity was checked by gel electrophoresis and UV-vis spectroscopy. High performance liquid chromatography (HPLC) determined the molecular weight of intact Phycocyanin to be 215 kDa, whereas denaturing gel electrophoresis showed the presence of two bands of 19 and 20 kDa molecular mass, indicating the characteristic (αβ) 6 subunit assembly of Phycocyanin. Zinc-assisted fluorescence enhancement further confirmed that both subunits are bilin-linked polypeptides.

Clive J. Barwell - One of the best experts on this subject based on the ideXlab platform.

  • Purification and characterization of Phycocyanin from the marine cyanobacterium Synechococcus sp. IO9201
    Plant Science, 1998
    Co-Authors: Julio Abalde, Liliana Betancourt, Enrique Torres, Ángeles Cid, Clive J. Barwell
    Abstract:

    This paper describes a suitable method for the optimum extraction and isolation of Phycocyanin from the cyanobacterium Synechococcus sp. IO9201 isolated from Caribbean waters. Phycocyanin from this microorganism was purified to homogeneity and some of its properties were investigated. The purification steps consisted of extraction, hydrophobic interaction chromatography and ion exchange chromatography. Freezing at −21°C-thawing at 4°C, using an alkaline buffer was the best method for extracting Phycocyanin from Synechococcus sp. IO9201. The best extraction was obtained using butyl-sepharose resin for hydrophobic interaction chromatography and 0.05 M Tris-HCl (pH = 7) containing 10% ethanol for Phycocyanin elution. Finally, Phycocyanin was further purified by ion exchange chromatography using Q-sepharose and eluted with a complex isocratic system. The estimated molecular weight of the Phycocyanin purified from Synechococcus sp. IO9201 was 102 000 daltons by gel filtration and the isoelectric point was 4.6. When analyzed by SDS-PAGE, Synechococcus sp. IO9201 Phycocyanin migrated as two bands having an apparent molecular weight of 21 360 and 18 980 Da. The first band corresponds to β Phycocyanin subunits, whereas the second corresponds to α Phycocyanin subunits. So, this Phycocyanin was characterized as (αCPCβCPC)3.

Chengtao Wang - One of the best experts on this subject based on the ideXlab platform.

  • Phycocyanin Exerts Anti-Proliferative Effects through Down-Regulating TIRAP/NF-κB Activity in Human Non-Small Cell Lung Cancer Cells.
    Cells, 2019
    Co-Authors: Shuai Hao, Jing Wang, Yan Yan, Jiawen Zhang, Yuqing Ren, Liyun Liu, Chengtao Wang
    Abstract:

    Phycocyanin is a type of marine functional food additive, exerting a health care efficacy with no side effects. It has been shown that Phycocyanin possesses anticancer function in non-small cell lung cancer (NSCLC) cells, but the underlying regulatory mechanism still remains unclear. Further investigation on the antineoplastic mechanism of Phycocyanin would provide useful information on NSCLC treatment. In this study, we explored the in vitro function and mechanism of Phycocyanin in three typical NSCLC cell lines, H1975, H1650, and LTEP-a2, for the first time. Phenotypic experiments showed that Phycocyanin significantly induced the apoptosis as well as suppressed the growth of NSCLC cells. Transcriptome analysis suggested that toll/interleukin 1 receptor domain-containing adaptor protein (TIRAP) was significantly down-regulated by Phycocyanin. Strikingly, similar to Phycocyanin-treated assays, siRNA knockdown of TIRAP expression also resulted in the anti-proliferative phenomenon in NSCLC cells. In addition, the activity of NF-κB signaling was also suppressed after silencing TIRAP expression, revealing that Phycocyanin exerted anti-proliferative function through down-regulating TIRAP/NF-κB activity in NSCLC cells. Collectively, this study has laid a theoretical basis on the treatment of NSCLC and the potential utilization of marine functional products.

  • Phycocyanin exerts anti proliferative effects through down regulating tirap nf κb activity in human non small cell lung cancer cells
    Cells, 2019
    Co-Authors: Shuai Hao, Jing Wang, Yan Yan, Jiawen Zhang, Yuqing Ren, Liyun Liu, Chengtao Wang
    Abstract:

    Phycocyanin is a type of marine functional food additive, exerting a health care efficacy with no side effects. It has been shown that Phycocyanin possesses anticancer function in non-small cell lung cancer (NSCLC) cells, but the underlying regulatory mechanism still remains unclear. Further investigation on the antineoplastic mechanism of Phycocyanin would provide useful information on NSCLC treatment. In this study, we explored the in vitro function and mechanism of Phycocyanin in three typical NSCLC cell lines, H1975, H1650, and LTEP-a2, for the first time. Phenotypic experiments showed that Phycocyanin significantly induced the apoptosis as well as suppressed the growth of NSCLC cells. Transcriptome analysis suggested that toll/interleukin 1 receptor domain-containing adaptor protein (TIRAP) was significantly down-regulated by Phycocyanin. Strikingly, similar to Phycocyanin-treated assays, siRNA knockdown of TIRAP expression also resulted in the anti-proliferative phenomenon in NSCLC cells. In addition, the activity of NF-κB signaling was also suppressed after silencing TIRAP expression, revealing that Phycocyanin exerted anti-proliferative function through down-regulating TIRAP/NF-κB activity in NSCLC cells. Collectively, this study has laid a theoretical basis on the treatment of NSCLC and the potential utilization of marine functional products.