Laccases stabilization with phosphatidylcholine liposomes

Abstract

Enzymes are globular proteins whose catalytic function is due to their three dimensional struc- ture. For this reason, stability strategies make use of compounds that avoid dismantling or distorting protein 3D structures. This study is concerned with the use of microencapsulation techniques to optimize enzyme stabilization. La- ccases were embedded in phophatidylcholine liposomes and their encapsulation capacity was assessed. Their enzymatic activity and stability were analyzed, comparing free-enzymes, enzy- mes in liposomes, and the lipid fraction sepa- rated from the aqueous fraction. An increase in their encapsulation efficiency was found at higher lipid/laccase ratios. Relative activity of enzyme-containing vesicles has also been shown to be retained much more than that of free native enzymes. The loss of activity of laccases en- trapped in the vesicles in the total stability process is lower than 10% compared with 40% to 60% of loss of free-laccases after heating the samples for 3 days. Laccase stabilization could be of interest to future textile or cosmetic appli- cations because of their potential for environ- mentally friendly oxidation technologies. Keywords: MLV Liposome; Enzymes; Laccas