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Ariff Arbakariya - One of the best experts on this subject based on the ideXlab platform.

  • Optimization of an induction strategy for improving Interferon-α2b production in the periplasm of Escherichia coli using response surface methodology
    'Portland Press Ltd.', 2010
    Co-Authors: Azaman, Siti Nor Ani, Ramakrishnan Nagasundara Ramanan, Tan, Joo Shun, Abdul Rahim Raha, Abdullah, Mohd Puad, Ariff Arbakariya
    Abstract:

    Induction strategies for the periplasmic production of recombinant human IFN-Alpha2b (Interferon-Alpha2b) by recombinant Escherichia coli Rosetta-gami 2(DE3) were optimized in shake-flask cultures using response surface methodology based on the central composite design. The factors included in the present study were induction point, which related to the attenuance of the cell culture, IPTG (isopropyl beta-D-thiogalactoside) concentration and induction temperature. Second-order polynomial models were used to correlate the abovementioned factors to soluble periplasmic IFN-Alpha2b formation and percentage of soluble IFN-Alpha2b translocated to the periplasmic space of E. coli. The models were found to be significant and subsequently validated. The proposed induction strategies consisted of induction at an attenuance of 4 (measured as D600), IPTG concentration of 0.05 mM and temperature of 25 degrees C. The optimized induction strategy reduced inclusion-body formation as evidenced by electron microscopy and yielded 323.8 ng/ml of IFN-Alpha2b in the periplasmic space with translocation of 74% of the total soluble product. In comparison with the non-optimized condition, soluble periplasmic production and the percentage of soluble IFN-Alpha2b translocated to the periplasmic space obtained in optimized induction strategies were increased by approx. 20-fold and 1.4-fold respectively

Spivak Nia - One of the best experts on this subject based on the ideXlab platform.

  • production of purified human recombinant Alpha2b Interferon
    Mikrobiolohichnyĭ zhurnal, 2012
    Co-Authors: A I Melnik, N M Zholobak, Spivak Nia
    Abstract:

    Technology for producing biologically active recombinant Alpha2b-Interferon is based on creating a bacterial producer strain containing the cDNA of human Interferon alpha. The authors have obtained two producers of recombinant Alpha2b-Interferon, the synthesis of the target protein in them occurs in the inclusion bodies. The schemes of isolation and purification of biologically active recombinant Alpha2b-Interferon have been developed. The drug purity was approximately 97-98%. Biological activity in the culture of sensory cells in the cytopathic test was 4.2*10(8)ME/mg.

Azaman, Siti Nor Ani - One of the best experts on this subject based on the ideXlab platform.

  • Optimization of an induction strategy for improving Interferon-α2b production in the periplasm of Escherichia coli using response surface methodology
    'Portland Press Ltd.', 2010
    Co-Authors: Azaman, Siti Nor Ani, Ramakrishnan Nagasundara Ramanan, Tan, Joo Shun, Abdul Rahim Raha, Abdullah, Mohd Puad, Ariff Arbakariya
    Abstract:

    Induction strategies for the periplasmic production of recombinant human IFN-Alpha2b (Interferon-Alpha2b) by recombinant Escherichia coli Rosetta-gami 2(DE3) were optimized in shake-flask cultures using response surface methodology based on the central composite design. The factors included in the present study were induction point, which related to the attenuance of the cell culture, IPTG (isopropyl beta-D-thiogalactoside) concentration and induction temperature. Second-order polynomial models were used to correlate the abovementioned factors to soluble periplasmic IFN-Alpha2b formation and percentage of soluble IFN-Alpha2b translocated to the periplasmic space of E. coli. The models were found to be significant and subsequently validated. The proposed induction strategies consisted of induction at an attenuance of 4 (measured as D600), IPTG concentration of 0.05 mM and temperature of 25 degrees C. The optimized induction strategy reduced inclusion-body formation as evidenced by electron microscopy and yielded 323.8 ng/ml of IFN-Alpha2b in the periplasmic space with translocation of 74% of the total soluble product. In comparison with the non-optimized condition, soluble periplasmic production and the percentage of soluble IFN-Alpha2b translocated to the periplasmic space obtained in optimized induction strategies were increased by approx. 20-fold and 1.4-fold respectively

Ramakrishnan Nagasundara Ramanan - One of the best experts on this subject based on the ideXlab platform.

  • Optimization of an induction strategy for improving Interferon-α2b production in the periplasm of Escherichia coli using response surface methodology
    'Portland Press Ltd.', 2010
    Co-Authors: Azaman, Siti Nor Ani, Ramakrishnan Nagasundara Ramanan, Tan, Joo Shun, Abdul Rahim Raha, Abdullah, Mohd Puad, Ariff Arbakariya
    Abstract:

    Induction strategies for the periplasmic production of recombinant human IFN-Alpha2b (Interferon-Alpha2b) by recombinant Escherichia coli Rosetta-gami 2(DE3) were optimized in shake-flask cultures using response surface methodology based on the central composite design. The factors included in the present study were induction point, which related to the attenuance of the cell culture, IPTG (isopropyl beta-D-thiogalactoside) concentration and induction temperature. Second-order polynomial models were used to correlate the abovementioned factors to soluble periplasmic IFN-Alpha2b formation and percentage of soluble IFN-Alpha2b translocated to the periplasmic space of E. coli. The models were found to be significant and subsequently validated. The proposed induction strategies consisted of induction at an attenuance of 4 (measured as D600), IPTG concentration of 0.05 mM and temperature of 25 degrees C. The optimized induction strategy reduced inclusion-body formation as evidenced by electron microscopy and yielded 323.8 ng/ml of IFN-Alpha2b in the periplasmic space with translocation of 74% of the total soluble product. In comparison with the non-optimized condition, soluble periplasmic production and the percentage of soluble IFN-Alpha2b translocated to the periplasmic space obtained in optimized induction strategies were increased by approx. 20-fold and 1.4-fold respectively

Tan, Joo Shun - One of the best experts on this subject based on the ideXlab platform.

  • Optimization of an induction strategy for improving Interferon-α2b production in the periplasm of Escherichia coli using response surface methodology
    'Portland Press Ltd.', 2010
    Co-Authors: Azaman, Siti Nor Ani, Ramakrishnan Nagasundara Ramanan, Tan, Joo Shun, Abdul Rahim Raha, Abdullah, Mohd Puad, Ariff Arbakariya
    Abstract:

    Induction strategies for the periplasmic production of recombinant human IFN-Alpha2b (Interferon-Alpha2b) by recombinant Escherichia coli Rosetta-gami 2(DE3) were optimized in shake-flask cultures using response surface methodology based on the central composite design. The factors included in the present study were induction point, which related to the attenuance of the cell culture, IPTG (isopropyl beta-D-thiogalactoside) concentration and induction temperature. Second-order polynomial models were used to correlate the abovementioned factors to soluble periplasmic IFN-Alpha2b formation and percentage of soluble IFN-Alpha2b translocated to the periplasmic space of E. coli. The models were found to be significant and subsequently validated. The proposed induction strategies consisted of induction at an attenuance of 4 (measured as D600), IPTG concentration of 0.05 mM and temperature of 25 degrees C. The optimized induction strategy reduced inclusion-body formation as evidenced by electron microscopy and yielded 323.8 ng/ml of IFN-Alpha2b in the periplasmic space with translocation of 74% of the total soluble product. In comparison with the non-optimized condition, soluble periplasmic production and the percentage of soluble IFN-Alpha2b translocated to the periplasmic space obtained in optimized induction strategies were increased by approx. 20-fold and 1.4-fold respectively