The use of pressure to modify enzyme activity in reversed micelles.
Pressurization 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, alpha-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 discussed.
Department of Chemical Engineering, Tulane University, New Orleans, Louisiana 70118.
A M
AM
Rao
N
N
Kommareddi
V T
VT
John
D001709:Biotechnology; D002918:Chymotrypsin / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D005030:Ethylenes; D005740:Gases; D066298:In Vitro Techniques; D008049:Lipase / Q000378:metabolism; D008823:Micelles; D011312:Pressure; D013055:Spectrophotometry, Infrared; D014978:Xenon
D004798:Enzymes; D005030:Ethylenes; D005740:Gases; D008823:Micelles; D014978:Xenon; C036216:ethylene; D008049:Lipase; D002918:Chymotrypsin