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Selective separation of trypsin from pancreatin using bioaffinity in reverse micellar system composed of a nonionic surfactant
Author(s) -
Adachi Motonari,
Shibata Kengo,
Shioi Akihisa,
Harada Makoto,
Katoh Shigeo
Publication year - 1998
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(19980620)58:6<649::aid-bit11>3.0.co;2-2
Subject(s) - trypsin , pulmonary surfactant , chromatography , chemistry , micelle , biochemistry , enzyme , organic chemistry , aqueous solution
Selective separation of trypsin from a mixture involving many kinds of contaminating proteins, i.e., pancreatin, was achieved using trypsin inhibitor immobilized in the reverse micelles, which were composed of a nonionic surfactant, tetra‐oxyethylene monodecylether. To determine the efficient operations throughout the whole separation process we examined the operating conditions, which affect the immobilization efficiency of trypsin inhibitor and also the forward and backward extractions of trypsin. Fifty percent of the recovery of trypsin from pancreatin was realized with no loss of activity of the recovered trypsin. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58: 649–653, 1998.