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 ex amined the operating conditions, which affect the immobilization effic iency of trypsin inhibitor and also the forward and backward extractio ns of trypsin. Fifty percent of the recovery of trypsin from pancreati n was realized with no loss of activity of the recovered trypsin. (C) 1998 John Wiley & Sons, Inc.