Influence of counter anion of ionic liquids on the packaging of pepsin

Abstract

Ionic liquids (ILs) are innovative solvents that have gained more attention because of their tunable features, which have been designed to facilitate sustainable chemistry. Due to their polar nature, they are studied for the dissolution of many biological components and in many cases it can stabilize them. In this framework, the effect of concentration and anion of ILs on stability of pepsin are analyzed. Pepsin's structural stability under imidazolium substituted ILs ([C4mim][Cl]; [C4mim][BF4] and [C4mim][PF6]) concentrations was investigated through spectral techniques such as UV–vis, fluorescence emission and lifetime studies. The outcomes of the research indicate that the concentration of ILs can significantly affect the stability or instability of a specific protein. Further the activity of enzyme has been analyzed through proteolytic activity of BSA where Pepsin + aq. ILs act as a protease. These activities are examined through polarized optical microscopic studies and change in emission after addition of protease. Such findings can be verdict as an alternative route for therapeutics.