مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Verion

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

698
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

320
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

Increasing the Catalytic Power of the Flavin Reductase DszD Enzyme Using Site-Directed Mutagenesis Method in Rhodococcus Erythropolis

Pages

  68-77

Abstract

 Background and Aim The Flavin reductase DszD enzyme is a key enzyme for providing required reduction potential in the Bacterial desulfurization process. Considering the low speed of desulfurization process because of low Catalytic power of this enzyme, it is necessary to increase the Catalytic power of flavin reductase for industrial use of this enzyme as biocatalyst. Methods & Materials The three-dimensional structure of the Flavin reductase DszD enzyme was predicted by a CPHmodel server and its amino acid sequence was searched in the protein data bank to identify the homologue molecules. Based on the alignment of the amino acid sequence and the model molecules, the key residues at the flavin mononucleotide substrate were identified. The key residue of asparagine at position 77 was replaced with phenylalanine using the site-directed mutagenesis method. Ethical Considerations This study with research ethics code IR. NIGEB. EC. 1398. 6. 24 A has been approved by research ethics committee at National Institute of Genetic Engineering and Biotechnology, Tehran, Iran. Results The cloning and expression of each of the wild-type and mutant genes were performed separately. The Catalytic power of the produced wild-type and mutant enzymes were compared. The catalytic activity measurements showed that the mutant enzyme had a 2. 5 fold increase in Catalytic power. Conclusion Replacing phenylalanine with asparagine at position 77 of Flavin reductase DszD enzyme leads to an increase in enzyme Catalytic power to increase the speed of Bacterial desulfurization process.

Cites

  • No record.
  • References

    Cite

    APA: Copy

    Fallahzadeh, Ramin, ESFAHANI, KASRA, AKHAVAN SEPAHI, ABBAS, KAMALI, NASRIN, & BAMBAI, BIJAN. (2019). Increasing the Catalytic Power of the Flavin Reductase DszD Enzyme Using Site-Directed Mutagenesis Method in Rhodococcus Erythropolis. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), 22(5 ), 68-77. SID. https://sid.ir/paper/69171/en

    Vancouver: Copy

    Fallahzadeh Ramin, ESFAHANI KASRA, AKHAVAN SEPAHI ABBAS, KAMALI NASRIN, BAMBAI BIJAN. Increasing the Catalytic Power of the Flavin Reductase DszD Enzyme Using Site-Directed Mutagenesis Method in Rhodococcus Erythropolis. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ)[Internet]. 2019;22(5 ):68-77. Available from: https://sid.ir/paper/69171/en

    IEEE: Copy

    Ramin Fallahzadeh, KASRA ESFAHANI, ABBAS AKHAVAN SEPAHI, NASRIN KAMALI, and BIJAN BAMBAI, “Increasing the Catalytic Power of the Flavin Reductase DszD Enzyme Using Site-Directed Mutagenesis Method in Rhodococcus Erythropolis,” ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), vol. 22, no. 5 , pp. 68–77, 2019, [Online]. Available: https://sid.ir/paper/69171/en

    Related Journal Papers

    Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops






    Move to top
    telegram sharing button
    whatsapp sharing button
    linkedin sharing button
    twitter sharing button
    email sharing button
    email sharing button
    email sharing button
    sharethis sharing button