Modification of enzyme activity in reversed micelles through clathrate hydrate formation.
The physical phenomenon of clathrate hydrate formation in protein-containing reversed micelles is described. Hydrate formation in reversed micelles is a method of adjusting the water to surfactant molar ratio, wo, which influences micellar size. Lipase and alpha-chymotrypsin encapsulated in large reversed micelles of high wo show significant enhancements in activity when the micelle size is reduced through hydrate formation. Alternate methods of micelle size adjustments also show enhancements in activity. The implications for improving the activity of such encapsulated enzymes recovered from fermentation media through phase transfer into reversed micelles are discussed.
Department of Chemical Engineering, Tulane University, New Orleans 70118.
A M
AM
Rao
H
H
Nguyen
V T
VT
John
D002918:Chymotrypsin / Q000378:metabolism*; D003080:Cold Temperature; D008049:Lipase / Q000378:metabolism*; D008823:Micelles; D011312:Pressure; D014867:Water / Q000737:chemistry / Q000378:metabolism*
D008823:Micelles; D014867:Water; D008049:Lipase; D002918:Chymotrypsin