title: Enhanced enzymatic thermal stability and activity in functionalized mesoporous silica monitored by (31) p NMR.
abstract: Organophosphorus hydrolase (OPH) is immobilized on ammonium-modified mesoporous silica particles. Thermal stability and activity are measured with a (31) P NMR assay of the conversion of paraoxon (toxic) to its non-toxic hydrolysis product. After immobilization, OPH is significantly more active at room temperature and retained activity even after being heated to 45 °C for 1 month.
authors.affiliation: Department of Chemistry, University of Vermont, 82 University Place, Burlington, VT 05405, USA.
authors.forename: Kheireddine
authors.initials: K
authors.lastname: El-Boubbou
authors.forename: David A
authors.initials: DA
authors.lastname: Schofield
authors.forename: Christopher C
authors.initials: CC
authors.lastname: Landry
mesh_terms: D043303:Aryldialkylphosphatase / Q000737:chemistry*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008422:Materials Testing; D010759:Phosphorus Isotopes / Q000032:analysis; D016062:Porosity; D012822:Silicon Dioxide / Q000737:chemistry*; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D010759:Phosphorus Isotopes; D012822:Silicon Dioxide; D043303:Aryldialkylphosphatase