Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heter...

• Author(s): Gomes, Daniela S. ; Matamá, Maria Teresa ; Paulo, Artur Cavaco ; Jordão, R. C. C. ; Takaki, G. M. Campos ; Salgueiro, Alexandra A.
• Date: 2013
• Persistent ID: http://hdl.handle.net/1822/28718
• Origin: RepositóriUM - Universidade do Minho
• Subject(s): Heterologous cutinase; Enzyme stabilization
• Document Type: Conference Object
• Language: English

Description

Cutinases (EC 3.1.1.74)are versatile enzymes that have hydrolytic activity on various esters [1]. The spacial structure and the catalytic site of the enzymes can be protected by chemical additives to promove the stability of the activity [2, 3]. The goal of this work was to improve the stability of a recombinant cutinase produced by Escherichia coli.