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Separation of MBP Fusion Proteins through Affinity Membranes
Author(s) -
Cattoli Francesca,
Sarti Giulio C.
Publication year - 2002
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp010119r
Subject(s) - membrane , microporous material , chromatography , chemistry , fusion , maltose binding protein , affinity chromatography , kinetics , matrix (chemical analysis) , fusion protein , biochemistry , recombinant dna , organic chemistry , philosophy , linguistics , gene , enzyme , physics , quantum mechanics
Abstract Cellulose microporous membranes have been modified in order to obtain a stationary phase specific for the recovery of a class of fusion proteins containing the maltose binding protein domain, through affinity chromatography separations. The feasibility of a single step separation process for the recovery of large amounts of the desired product has been considered. To that purpose, a preparative scale module has been realized, suitable for flat sheet membranes. The affinity matrix used proved to be highly selective toward the fusion proteins examined. The binding capacity determined is comparable with the nominal binding capacity of commercially available supports. The influence of the relevant working parameters, such as flow rate, on the performances of the recovery process has been studied.