Abstract
A simple, cost-efficient method for purification of E. coli-derived recombinant Taq DNA polymerase isolated from the thermophilic bacterium Thermus aquaticus is described. Recombinant Taq DNA polymerase was purified using an aqueous two-phase extraction method following a primary treatment of heat denaturation. The extraction method selectively enriched Taq DNA polymerase in the lower salt phase with complete recovery and high specific activity. The purified Taq DNA polymerase protein displayed nearly eightfold purification with ∼117 % activity recovery with an insignificant amount of host DNA. This process was found to be rapid and scalable in comparison to the conventional ammonium sulfate precipitation method.