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• W156004564 abstract "The one step purification to homogeneity using immobilized metal ion affinity chromatography (IMAC) of a recombinant cyclodextrin glycosyl transferase (rCGTase) from alkalophillic Bacillus cloned in Escherichia coli is described. Tandem columns with copper and zinc were used. Negative affinity on Zn(II) and positive affinity on Cu(II) were observed. We compared this pseudobiospecific affinity chromatography technique with the biospecific affinity chromatography using β cyclodextrin (CD) as the immobilized ligand in terms of purification factor and activity recovery. We obtained the same purification factor in both cases but with 79% activity recovery with the β CD ligand against 89% enzymatic activity recovery for IMAC. No further treatment of the enzyme was necessary for pseudobiospecific affinity chromatography because the elution conditions used did not inhibit the enzyme, as opposed to the biospecific approach. The presence of 10 mg/ml of β CD or 150 mM of β-D-glucose in the adsorption buffer did not disturb rCGTase adsorption on Cu(U) columns. These facts suggested that at least one histidine outside of the active site is accessible on the surface of the rCGTase molecule for binding on Cu(II)." @default.
• W156004564 created "2016-06-24" @default.
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• W156004564 date "1996-01-01" @default.
• W156004564 modified "2023-09-24" @default.
• W156004564 title "One-Step Affinity Purification of a Recombinant Cyclodextrin Glycosyl Transferase By (Cu(II), Zn(II) Tandem Column) Immobilized Metal Ion Affinity Chromatography" @default.
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• W156004564 doi "https://doi.org/10.1016/s1569-2558(08)60133-2" @default.
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