• DocumentCode
    2510793
  • Title

    Improving the Stability of Cellulase by Immobilization on Chitosan-Coated Magnetic Nanoparticles Modified alpha-Ketoglutaric Acid

  • Author

    Zhou, Yu-Ting ; Su, Sai-Nan ; Song, Ming-Min ; Nie, Hua-Li ; Zhu, Li-Min ; Branford-White, Christopher J.

  • Author_Institution
    Coll. of Chem., Chem. Eng. & Biotechnol., Donghua Univ., Shanghai, China
  • fYear
    2009
  • fDate
    11-13 June 2009
  • Firstpage
    1
  • Lastpage
    4
  • Abstract
    The application of cellulases in various industries demands highly stable enzymes, able to perform at extreme pH values and temperatures. In this study, the cellulase, which was immobilized on the chitosan-coated magnetic nanoparticles modified with alpha-ketoglutaric acid (alpha-KA-CCMNPs), exhibited a broader pH range of high activity and the loss of the activity of immobilized cellulase was lower than that of free cellulase. And the optimal temperature for immobilized cellulase was 50degC, whereas that for free cellulase was 40degC. Meanwhile, the immobilized cellulase showed better thermal stability than free cellulase at high temperature range. In addition, the storage stability of the cellulase was improved greatly after it was immobilized on the surface of alpha-KA-CCMNPs.
  • Keywords
    biothermics; enzymes; magnetic particles; molecular biophysics; nanoparticles; pH; thermal stability; alpha-KA-CCMNP; alpha-ketoglutaric acid; cellulase stability; chitosan-coated magnetic nanoparticle; pH value; stable enzyme; storage stability; temperature 40 degC; temperature 50 degC; thermal stability; Biochemistry; Chemicals; Magnetic materials; Magnetic separation; Nanoparticles; Stability; Sugar; Surface resistance; Temperature; Textile industry;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Bioinformatics and Biomedical Engineering , 2009. ICBBE 2009. 3rd International Conference on
  • Conference_Location
    Beijing
  • Print_ISBN
    978-1-4244-2901-1
  • Electronic_ISBN
    978-1-4244-2902-8
  • Type

    conf

  • DOI
    10.1109/ICBBE.2009.5162941
  • Filename
    5162941