doi:10.1128/AEM.70.2.1249-1251.2004engAbian,O.Grazú,V.Hermoso,J.González,R.García,J. L.Fernández-Lafuente,R.Guisán,J. M.Stabilization of Penicillin G Acylase from Escherichia coli: Site-Directed Mutagenesis of the Protein Surface to Increase Multipoint Covalent AttachmentART-2004-86285Three 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.2004http://zaguan.unizar.es/record/6916310.1128/AEM.70.2.1249-1251.2004http://zaguan.unizar.es/record/69163oai:zaguan.unizar.es:69163info:eu-repo/grantAgreement/ES/CICYT/BIO2000-0747-C05-02info:eu-repo/grantAgreement/ES/CICYT/BIO2001-2259APPLIED AND ENVIRONMENTAL MICROBIOLOGY 70, 2 (2004), 1249-1251All rights reservedhttp://www.europeana.eu/rights/rr-f/info:eu-repo/semantics/openAccess