From Tritirachium album. Serine protease for proteolytic inactivation of nucleases during isolation of DNA and RNA. Proteinase K is a highly reactive serine protease that displays an 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 characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids. Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature when compared to native Proteinase K. Recombinant Proteinase K is expressed from yeast Pichia pastoris with cloned gene encoding Engyodontium album (Tritirachium album) endolytic protease.
