Rapid purification of two thermophilic proteinases using dye-ligand chromatography.

D A Cowan, R M Daniel

Index: J. Biochem. Biophys. Methods 32(1) , 1-6, (1996)

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Abstract

Dye-ligand chromatography has been used successfully for the purification of extracellular thermostable proteinases from thermophilic Bacillus and Thermus cultures. Single-step purification factors of up to 115-fold (for Thermus protease) and 2195-fold (for Bacillus protease) were obtained. Elution studies suggested that the mode of binding involved the enzyme active sites. The method was readily scalable to 600 1 volume.