Enhanced stability of laccase by xylitol

• Main Author: Zille, Andrea
• Publication Date: 2006
• Other Authors: Moldes, Diego, Irgoliç, Ramona, Paulo, Artur Cavaco
• Language: eng
• Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
• Download full: http://hdl.handle.net/1822/25286

Laccase is a multicopper oxidase able to perform one-electron oxidation of several aromatic substrates. The application of laccase on wood delignification, drug analysis, biosensor, wine clarification, bioremediation, etc., was proposed [1]. As every enzymatic system, laccase has some limitations due to the reaction conditions, mainly temperature and pH. Deactivation of laccase at pH values over 6 and lower 3 are undesirable properties that must be improved. The addition of some compounds is an easy and conventional way to get the stabilization of laccase [2]. In this work laccase from Trametes hirsuta was studied in order to get its stabilization towards different pH values by addition of xylitol, a polyol used in food industry with optimal characteristics with respect to its prize and non-toxical properties.