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Increasing the activity of immobilized enzymes with nanoparticle conjugation
Current Opinion in Biotechnology
  • Shaowei Ding, Iowa State University
  • Allison A. Cargill, Iowa State University
  • Igor L. Medintz, United States Naval Research Laboratory
  • Jonathan C. Claussen, Iowa State University
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The efficiency and selectivity of enzymatic catalysis is useful to a plethora of industrial and manufacturing processes. Many of these processes require the immobilization of enzymes onto surfaces, which has traditionally reduced enzyme activity. However, recent research has shown that the integration of nanoparticles into enzyme carrier schemes has maintained or even enhanced immobilized enzyme performance. The nanoparticle size and surface chemistry as well as the orientation and density of immobilized enzymes all contribute to the enhanced performance of enzyme–nanoparticle conjugates. These improvements are noted in specific nanoparticles including those comprising carbon (e.g., graphene and carbon nanotubes), metal/metal oxides and polymeric nanomaterials, as well as semiconductor nanocrystals or quantum dots.

This is a manuscript of an article from Current Opinion in Biotechnology 34 (2015): 242, doi:10.1016/j.copbio.2015.04.005.

Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.
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Shaowei Ding, Allison A. Cargill, Igor L. Medintz and Jonathan C. Claussen. "Increasing the activity of immobilized enzymes with nanoparticle conjugation" Current Opinion in Biotechnology Vol. 34 (2015) p. 242 - 250
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