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Proteinase K is a highly active 28,904-Da serine protease isolated from the fungus Tritirachium album. A highly reactive serine protease that displays the ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterised so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids.
The application of Proteinase K solution is similar to the Native Proteinase K and is used in the isolation or preparation of high molecular weight nucleic acids. However, this Proteinase K is highly pure and has a higher specific activity and is more stable at room temperature as compared to native Proteinase K. It is stable and active over a wide pH range of 4-12. Proteinase K is also active with SDS, urea and EDTA and the most active temperature is 65°C. It is inactivated by diisopropyl fluorophosphates (DFP) and phenyl methane sulfonyl fluoride (PMSF).
