Enzyme Activity Boosted by Entrapping in a Nanoporous Support

Rational design of organically functionalized nanoporosity could lead to new approaches to entrap and stabilize biomolecules for a wide range of applications.

The Science

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 research has just been published in the Journal of the American Chemical Society and was selected to be highlighted in the Science & Technology section of the September issue of Chemical & Engineering News.

Principal Investigator

Eric J. Ackerman

Co-Principal Investigator

Jun Liu


Lei, C., Y. Shin, J. Liu and E. J. Ackerman. 2002. “Entrapping Enzyme in a Functionalized Nanoporous Support,” Journal of the American Chemical Society 124(38). DOI:10.1021/ja026855o.