An enzyme derived from the fungus Tritirachium album and produced by expression in the yeast Pichia pastoris. Proteinase K has broad cleavage specificity, cleaves many proteins, and retains its stability in the presence of detergents and urea.

The enzyme exhibits high specific activity against double-stranded DNA, while single-stranded DNA or RNA remain intact under standard conditions.

Increasing the proportion of full-length cDNA by removing RNase H-like activity.

The recombinant Taq DNA polymerase has the 5'-3' DNA-dependent polymerase activity and the 5'-3' exonuclease activity of the native Taq DNA polymerase from Thermus aquaticus. The rate of advancement of Taq DNA polymerase depends on the complexity of the DNA template and is approximately 1.5-2 kb/min.