Abstract

It was shown that formate dehydrogenase (FDH) can be purified with affinity partitioning directly from the cell homogenate of Candida boidinii. The procedure is faster than the other methods known and scale-up is possible without apparent difficulties. The specific activity of the purified FDH was between 3.5 and 6 U/mg, depending on the disintegration method. The top phase containing the affinity ligand Procion Red HE3b coupled to PEG-6000 can be recycled directly at least four times without lowering significantly the quality of the product. The costs for the purification of FDH by affinity partition are comparable to other methods.

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