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      Rapid purification of two thermophilic proteinases using dye-ligand chromatography

      Cowan, Don A.; Daniel, Roy M.
      DOI
       10.1016/0165-022X(95)00028-P
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      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
      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 scaleable to 600 l volume.
      Date
      1996
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3069]
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