ISSN:
0006-3592
Keywords:
bioaffinity separation
;
pancreatin
;
trypsin
;
reverse micelles
;
nonionic surfactant
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
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