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Protein extraction and activity in reverse micelles of a nonionic detergent
Author(s) -
Ayala Guadalupe A.,
Kamat Sanjay,
Beckman Eric J.,
Russell Alan J.
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260390803
Subject(s) - micelle , extraction (chemistry) , chemistry , chromatography , biochemistry , organic chemistry , aqueous solution
Abstract We describe, for the first time, the ability of a polyoxyethylene sorbitan trioleate‐isopropanol microemulsion in hexane to solubilize pure proteins. The dependences of cytochrome c extraction and buffer solubilization by the reverse micellar system on ionic strength of the aqueous phase, detergent concentration, and cosurfactant concentration result in increased extraction. In addition, subtilisin (a serine protease) is shown to be active in this microemulsion. Further the activity of the enzyme can be regulated by the water content of the micelles, enabling control of enzyme activity by “solvent engineering.”