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Modification of Enzyme Activity in Reversed Micelles through Clathrate Hydrate Formation
Author(s) -
Rao A. Madhusudhan,
Nguyen Huyen,
Johnn Vijay T.
Publication year - 1990
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00006a009
Subject(s) - micelle , chemistry , hydrate , pulmonary surfactant , clathrate hydrate , lipase , chemical engineering , chromatography , enzyme , organic chemistry , aqueous solution , biochemistry , engineering
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, w o , which influences micellar size. Lipase and α‐chymotrypsin encapsulated in large reversed micelles of high w o 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.