69163 20180228135116.0 doi 10.1128/AEM.70.2.1249-1251.2004 sideral 86285 ART-2004-86285 eng (orcid)0000-0001-5664-1729 Abian,O. Stabilization of Penicillin G Acylase from Escherichia coli: Site-Directed Mutagenesis of the Protein Surface to Increase Multipoint Covalent Attachment 2004 Access copy available to the general public Unrestricted Three 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. info:eu-repo/grantAgreement/ES/CICYT/BIO2000-0747-C05-02 info:eu-repo/grantAgreement/ES/CICYT/BIO2001-2259 info:eu-repo/semantics/openAccess All rights reserved http://www.europeana.eu/rights/rr-f/ 3.81 2004 MICROBIOLOGY 17 / 84 = 0.202 2004 Q1 T1 BIOTECHNOLOGY & APPLIED MICROBIOLOGY 16 / 131 = 0.122 2004 Q1 T1 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Grazú,V. Hermoso,J. González,R. García,J. L. Fernández-Lafuente,R. Guisán,J. M. 70, 2 (2004), 1249-1251 Appl. environ. microbiol. APPLIED AND ENVIRONMENTAL MICROBIOLOGY 0099-2240 62141 http://zaguan.unizar.es/record/69163/files/texto_completo.pdf Versión publicada 136400 http://zaguan.unizar.es/record/69163/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:69163 driver articulos 2018-02-28-10:22:56 ARTICLE