| 研究実績の概要 |
My research focused on establishing an isothermal recombinase polymerase amplification (RPA), a method conducted at around 41°C, utilizing recombinase, single-stranded DNA binding protein, strand-displacing DNA polymerase, and an ATP regenerating enzyme. I engineered a pyruvate kinase (Tma-PK) from thermophilic bacterium Thermotoga maritima as the ATP regenerating enzyme in RPA. I successfully optimized lyophilization conditions for RPA. The lyophilized RPA reagents remained stable for over 28 days at room temperature. RPA reagents containing Tma-PK exhibited superior performance to those with human PK suggesting that thermostable enzymes are preferable to mesophilic ones in RPA. I disseminated these findings in two domestic conferences and published two peer-reviewed articles.
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