Pilot scale affinity chromatography: Purification of β‐galactosidase | Zendy

Robinson P. J. | Zendy; Wheatley M. A. | Zendy; Janson J.C. | Zendy; Dunnill P. | Zendy; Lilly M. D. | Zendy

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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.

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