Stabilization of Enzyme by Using Hydrophobic Ligands

Abstract

The protection (stabilization) effect of various hydrophobic ligands on the denaturation and aggregation of carbonic anhydrase from bovine (CAB) has been quantitatively investigated under various heat stress conditions. In a limited temperature range (40∼60°C), where the protein was only partially denatured and the local hydrophobicities (LH) of CAB were positive effective stabilization of the protein is achieved by the addition of various ligands. The importance of balance between hydrophobic head and hydrophilic tail of the ligands is hypothesized.