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The large fragment of DNA polymerase I from  Geobacillus stearothermophilus  GIM1.543 (Bst DNA polymerase) with 5′-3′ DNA polymerase activity while in absence of 5′-3′ exonuclease activity possesses high thermal stability and polymerase activity. Bst DNA polymerase was employed in isothermal multiple self-matching initiated amplification (IMSA) which amplified the interest sequence with high selectivity and was widely applied in the rapid detection of human epidemic diseases. However, the detailed information of commercial Bst DNA polymerase is unpublished and well protected by patents, which makes the high price of commercial kits. In this study, wild-type Bst DNA polymerase (WT) and substitution mutations for improving the efficiency of DNA polymerization were expressed and purified in  E. coli . Site-directed substitutions of four conserved residues (Gly 310 , Arg 412 , Lys 416 , and Asp 540 ) in the activity site of Bst DNA polymerase influenced efficiency of polymerizing dNTPs. The substitution of residue Gly 310  by alanine or leucine and residue Asp 540  by glutamic acid increased the efficiency of polymerase activity. All mutants with higher polymerizing efficiency were employed to complete the rapid detection of EV71-associated hand, foot, and mouth disease (HFMD) by IMSA approach with relatively shorter period which is suitable for the primary diagnostics setting in rural and underdeveloped areas.

biomed research international

Enhancement of Polymerase Activity of the Large Fragment in DNA Polymerase I from<i>Geobacillus stearothermophilus</i>by Site-Directed Mutagenesis at the Active Site

Enhancement of Polymerase Activity of the Large Fragment in DNA Polymerase I fromGeobacillus stearothermophilusby Site-Directed Mutagenesis at the Active Site