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

Abian,O. ; Grazú,V. ; Hermoso,J. ; González,R. ; García,J. L. ; Fernández-Lafuente,R. ; Guisán,J. M.

Resumen: 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.

Idioma: Inglés

DOI: 10.1128/AEM.70.2.1249-1251.2004

Año: 2004

Publicado en: APPLIED AND ENVIRONMENTAL MICROBIOLOGY 70, 2 (2004), 1249-1251
ISSN: 0099-2240

Factor impacto JCR: 3.81 (2004)

Categ. JCR: MICROBIOLOGY rank: 17 / 84 = 0.202 (2004) - Q1 - T1
Categ. JCR: BIOTECHNOLOGY & APPLIED MICROBIOLOGY rank: 16 / 131 = 0.122 (2004) - Q1 - T1

Financiación: info:eu-repo/grantAgreement/ES/CICYT/BIO2000-0747-C05-02
Financiación: info:eu-repo/grantAgreement/ES/CICYT/BIO2001-2259

Tipo y forma: Article (Published version)