The recombinant enzyme is a mutant to the native protease, which gains higher specific activity and yield as well as tolerance to a wider pH and temperature range. The large scale recombinant preparation has advantage in lot-to-lot consistency, superior purity and cost-efficiency. DNA-free nature of recombinant Proteinase K made it well-suited in isolating PCR and RT-PCR templates.
Crystal structure data indicate that the enzyme belongs to the subtilisin family, which is characterized by a catalytic triad (Asp39-His69-Ser224) in the active site.
Proteinase K does not exhibit pronounced cleavage specificity, and the preferred cleavage site is the peptide bond at hydrophobic amino acids.
