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:

197
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

79
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

Kinetic Study of Erythrose Reductase Extracted from Yarrowia lipolytica

Pages

  97-101

Abstract

 Erythritol as a non-caloric and non-cariogenic sweetener is safe for diabetics. Both microbial fermentation and chemical methods can be used to produce erythritol, but chemical methods failed to be industrialized due to their low efficiency. Moniliella tomentosa, Aureobasidium sp. and Yarrowia lipolytica are industrial producers of erythritol. Erythrose reductase (ER) is a key enzyme in the biosynthesis of erythritol and catalyzes the final step in this pathway. Enzyme extract was obtained from Y. lipolytica by grinding cells with 0. 5mm glass beads and ER activity was performed using 10 μ l enzyme extract, 7. 5 mM NADPH and 12 mM D-erythrose in potassium phosphate buffer (pH 7. 5). Reaction was monitored with decreasing of NADPH absorbance in OD340 at 37 ˚ C for 8 min by a microplate analyzer. In order to determine the activation energy (Ea), activity of enzyme was measured in 4-45 ˚ C and results were analyzed with Kinetic software according to Arrhenius equation. The best enzyme activity of ER was 6. 268 mU. One unit of ER activity was defined as the amount of enzyme that catalyzes the oxidation of 1μ mol of NADPH per minute. Specific activity of enzyme was equal to 3. 24U/mg and finally the Ea was determined to be 29. 6208 KJ. ER specific activity in this study was lower than the only similar study that used Y. lipolytica. Purification, overexpression and optimizing the reaction can help to increase enzyme performance.

Cites

  • No record.
  • References

    Cite

    APA: Copy

    Mohammadi Farsani, Masoud, MOHAMMADI, MOHAMMAD, GHEZELBASH, GHOLAM REZA, & SHAHRIARI, ALI. (2019). Kinetic Study of Erythrose Reductase Extracted from Yarrowia lipolytica. JOURNAL OF CELL AND MOLECULAR RESEARCH, 10(2), 97-101. SID. https://sid.ir/paper/329310/en

    Vancouver: Copy

    Mohammadi Farsani Masoud, MOHAMMADI MOHAMMAD, GHEZELBASH GHOLAM REZA, SHAHRIARI ALI. Kinetic Study of Erythrose Reductase Extracted from Yarrowia lipolytica. JOURNAL OF CELL AND MOLECULAR RESEARCH[Internet]. 2019;10(2):97-101. Available from: https://sid.ir/paper/329310/en

    IEEE: Copy

    Masoud Mohammadi Farsani, MOHAMMAD MOHAMMADI, GHOLAM REZA GHEZELBASH, and ALI SHAHRIARI, “Kinetic Study of Erythrose Reductase Extracted from Yarrowia lipolytica,” JOURNAL OF CELL AND MOLECULAR RESEARCH, vol. 10, no. 2, pp. 97–101, 2019, [Online]. Available: https://sid.ir/paper/329310/en

    Related Journal Papers

  • No record.
  • 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