Bioaffinity separation of trypsin using trypsin inhibitor immobilized in reverse micelles composed of a nonionic surfactant.
Trypsin inhibitor was converted to hydrophobic states by covalently combining cholesteryl groups using an acylation reaction, and was immobilized in reverse micelles composed of a nonionic surfactant. Using this reverse micellar phase containing trypsin inhibitor as an affinity ligand, trypsin was selectively separated with high recoveries from a mixture of several kinds of contaminating proteins by forward and backward extraction. No loss of activity of the recovered trypsin was observed through these operations. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 406-408, 1997.
Adachi
M
M
Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611, Japan.
Yamazaki
M
M
Harada
M
M
Shioi
A
A
Katch
S
S