kamyar khoshnevisan - Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability

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  Publication Details (including relevant citation   information):

  Chemical Engineering Journal
    Volume 171, Issue 2, 1 July 2011, Pages 669-673

  doi:10.1016/j.cej.2011.04.039  | How to Cite or Link Using DOI


  Cellulase on commercial superparamagnetic nanoparticles was   characterized by DLS, and TEM methods in relation to their size   and structure. The cellulase enzyme was bound via physical   adsorption (ionic bound). FTIR spectroscopy confirmed the   successful binding of cellulase (endoglucanase) onto the   particle, and binding efficiency was determined at 95% using the   Bradford method. The maximal enzyme activity was assessed using   CMC as the substrate and was 0.1 unit (μmol/min ml). The   adsorption capacity of cellulase onto nanoparticles reached 31   mg/g. The stability of the immobilized enzyme increased in   comparison with the free enzyme. Overall, this study showed that   that the stability and activity of the cellulase were enhanced   via physical adsorption to the magnetic nanoparticles. This   suggested that immobilized enzyme on magnetic beads could be used   in an interesting range of application allowing both using in   broader temperature and pH ranges, facilitating long-term   storage, while permitting magnetic recovery of the enzyme for   reuse or purification of the product.

  Address (URL): http://www.sciencedirect.com/science/article/pii/S1385894711005109