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Stabilization of Penicillin G Acylase from Escherichia coli: Site-Directed Mutagenesis of the Protein Surface To Increase Multipoint Covalent Attachment

AuthorsAbian, Olga ; Grazú, Valeria; Hermoso, Juan A. ; González García, Ramón ; García, José Luis ; Fernández-Lafuente, Roberto ; Guisán, José Manuel
Issue DateFeb-2004
PublisherAmerican Society for Microbiology
CitationApplied and Environmental Microbiology 70(2):1249-1251 (2004)
AbstractThree mutations on the penicillin acylase surface (increasing the number of Lys in a defined area) were performed. They did not alter the enzyme's stability and kinetic properties; however, after immobilization on glyoxyl-agarose, the mutant enzyme showed improved stability under all tested conditions (e.g., pH 2.5 at 4°C, pH 5 at 60°C, pH 7 at 55°C, or 60% dimethylformamide), with stabilization factors ranging from 4 to 11 compared with the native enzyme immobilized on glyoxyl-agarose.
Publisher version (URL)http://dx.doi.org/10.1128/AEM.70.2.1249-1251.2004
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