Amperometric Detection of Conformational Change of Proteins Using Immobilized-Liposome Sensor System.

An immobilized liposome electrode (ILE)-based sensor was developed to quantify conformational changes of the proteins under various stress conditions. The ILE surface was characterized by using a tapping-mode atomic force microscopy (TM-AFM) to confirm surface immobilization of liposome. The uniform layer of liposome was formed on the electrode.

AOT/isooctane reverse micelles with a microaqueous core act as protective shells for enhancing the thermal stability of Chromobacterium viscosum lipase.

According to the different environmental systems for lipase reactions, changes in thermal stability were investigated by employing the Chromobacterium viscosum lipase and a two-step series-type deactivation model. The half-life (6.81 h) of the lipase entrapped in reverse micelles at 70 °C was 9.

Thermal deactivation kinetics of Pseudomonas fluorescens lipase entrapped in AOT/isooctane reverse micelles.

Thermostability of the lipase (EC 3.1.1.