The Use of Pressure to Modify Enzyme Activity in Reversed Micelles

摘要

AbstractPressurization of enzyme‐containing AOT‐water‐isooctane reversed micelles with low molecular weight gases leads to markedly different responses in activity characteristics. Microbial lipases exhibit a total cutoff in activity with as low a pressure as 2 MPa and a remarkable activity regain with depressurization. The observation also holds for reaction in monophasic organic solvents. The protease, α‐chymotrypsin, is unaffected by pressurization until a critical pressure wherein micellar instability occurs. The use of pressure as a switch for lipase reaction in nonaqueous media is d