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Enzyme Activity Boosted by Entrapping in a Nanoporous Support
Published: September 18, 2002
Posted: September 30, 2002

The Pacific Northwest National Laboratory (PNNL) researchers have discovered that modifying the surfaces of the pores of the silica particles with carboxylate groups enhanced the activity of the enzyme organophosphorus hydrolase (OPH), which is widely used for treating poisonous agents. The researchers have demonstrated that immobilizing an enzyme in a functionalized nanoporous silica support increases the activity of the enzyme by a factor of four over the enzyme in an unfunctionalized support. Immobilization of enzymes enables their use in applications ranging from continuous treatment of environmental contaminants to use in biosensors. The activity of an immobilized enzyme generally is lower than that of the enzyme in solution. The carboxylate groups attract the OPH and hold it within the pores of the silica without affecting the activity of the enzyme solving this problem. The PNNL group is led by Eric J. Ackerman and Jun Liu. The research has just been published on line in the Journal of the American Chemical Society and was selected to be highlighted in the Science & Technology section of the September 9, 2002, issue of Chemical & Engineering News.

Contact: Marvin Frazier, SC-72, 3-5468
Topic Areas:

  • Research Area: Subsurface Biogeochemical Research

Division: SC-33.2 Biological Systems Science Division, BER
      (formerly SC-72 Life Sciences Division, OBER)


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