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Pilot scale affinity chromatography: Purification of β‐galactosidase
Author(s) -
Robinson P. J.,
Wheatley M. A.,
Janson J.C.,
Dunnill P.,
Lilly M. D.
Publication year - 1974
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/bit.260160810
Subject(s) - chromatography , agarose , ammonium sulfate , adsorption , chemistry , affinity chromatography , solenoid , enzyme , column chromatography , specific activity , biochemistry , organic chemistry , mechanical engineering , engineering
β‐Galactosidase has been purified from an ammonium sulfate precipitate of E. coli strain ML308 by biospecific adsorption on a column of agarose gel substituted with p ‐aminophenyl‐β‐ D ‐thiogalactopyranoside. The system described using a 1.8 liter column has a useful processing capacity of 3.8 × 10 6 units of β‐galactosidase per 2 hr cycle. This corresponds to about 5 g of pure enzyme. An electromechanical timing device operates a set of six solenoid valves and carries out a preset program consisting of sample application, washing, and elation operations.