title: Reversible denaturation of carbonic anhydrase provides a method for its adsorptive immobilization.
abstract: Palmityl-substituted sepharose 4B has been used for adsorptive immobilization of heat-denatured carbonic anhydrase. The native form of this enzyme does not show any affinity for binding to this hydrophobic support. However, through the process of denaturation-renaturation performed by heating and subsequent cooling of an enzyme solution in the presence of the matrix, it was possible to obtain a catalytically active immobilized preparation, which was used successfully in continuous catalytic transformations. It is suggested that this simple procedure may provide a convenient method of immobilization for proteins, which are not normally adsorbed on hydrophobic supports.
authors: Institute of Biochemistry and Biophysics, University of Tehran, P.O. Box: 13145-1384, Tehran, Iran.
authors: F
authors: F
authors: Azari
authors: M
authors: M
authors: Nemat-Gorgani
mesh_terms: D000327:Adsorption; D000818:Animals; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D011489:Protein Denaturation; D012685:Sepharose / Q000031:analogs & derivatives; D013499:Surface Properties
chemical_list: D004800:Enzymes, Immobilized; C034543:palmityl-sepharose; D012685:Sepharose; D002256:Carbonic Anhydrases