Selective separation of trypsin from pancreatin using bioaffinity in reverse micellar system composed of a nonionic surfactant.
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.
Adachi
M
M
Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611, Japan. adachi@iae.kyoto-u.ac.jp
Shibata
K
K
Shioi
A
A
Harada
M
M
Katoh
S
S
D000818:Animals; D003902:Detergents; D007700:Kinetics; D008823:Micelles; D010179:Pancreas / Q000201:enzymology; D010194:Pancreatin / Q000302:isolation & purification*; D011092:Polyethylene Glycols; D013501:Surface-Active Agents; D013552:Swine; D014357:Trypsin / Q000302:isolation & purification* / Q000378:metabolism; D014361:Trypsin Inhibitors
D003902:Detergents; D008823:Micelles; D013501:Surface-Active Agents; D014361:Trypsin Inhibitors; D011092:Polyethylene Glycols; C053131:dodecyltetraethylene glycol monoether; D010194:Pancreatin; D014357:Trypsin