title: Activity losses among T4 lysozyme variants after adsorption to colloidal silica.
abstract: Maintaining a specific molecular conformation is essential for the proper functioning of an enzyme. A substantial loss of catalytic activity can occur from the displacement caused by even a single amino acid substitution. Activity may also be lost as an enzyme undergoes a conformational change during adsorption. In this study, we investigated the effect of thermostability on the activities of three T4 lysozyme variants after adsorption to 9 nm colloidal silica particles. Less-stable T4 lysozyme variants lost more activity after adsorption than did more stable variants, apparently because they experienced more extensive structural alteration.
authors: Department of Bioresource Engineering, Oregon State University, Corvallis, Oregon, USA.
authors: C K
authors: CK
authors: Bower
authors: Q
authors: Q
authors: Xu
authors: J
authors: J
authors: McGuire
mesh_terms: D000327:Adsorption; D017122:Bacteriophage T4 / Q000201:enzymology*; D002384:Catalysis; D003001:Cloning, Molecular; D003102:Colloids; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012822:Silicon Dioxide
chemical_list: D003102:Colloids; D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D012822:Silicon Dioxide; D009113:Muramidase