Rapid purification of two thermophilic proteinases using dye-ligand chromatography
Cowan, D.A. & Daniel, R.M. (1996). Rapid purification of two thermophilic proteinases using dye-ligand chromatography. Journal of Biochemical and Biophysical Methods, 31(1-2), 31-37.
Permanent Research Commons link: https://hdl.handle.net/10289/4468
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 scaleable to 600 l volume.