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Bioaffinity separation of trypsin using trypsin inhibitor immobilized in reverse micelles composed of a nonionic surfactant
Author(s) -
Adachi Motonari,
Yamazaki Masaru,
Harada Makoto,
Shioi Aihisa,
Katch Shigeol
Publication year - 1997
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/(sici)1097-0290(19970220)53:4<406::aid-bit8>3.0.co;2-r
Subject(s) - trypsin , chemistry , micelle , pulmonary surfactant , acylation , chromatography , covalent bond , trypsin inhibitor , enzyme , biochemistry , organic chemistry , aqueous solution , catalysis
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. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 406–408, 1997.