Chembiochem. 2026 May 27;27(10):e202500892. doi: 10.1002/cbic.202500892.

ABSTRACT

Inorganic pyrophosphatases (PPases) are ubiquitously present in living organisms, where they prevent the pathological accumulation of inorganic pyrophosphate (PPi) in cells by catalyzing its efficient hydrolysis. This study reports the cloning, expression, and biochemical characterization of two novel thermostable soluble PPases derived from Thermoleophilia bacterium (PPase_Tba) and Thermoprotei archaeon (PPase_Tar). These enzymes demonstrate robust catalytic activity toward PPi, along with exceptional thermostability and pH tolerance, exhibiting optimal activity at 85°C and pH 8.5. Notably, they retain 60-70% of their maximal activity even at 25°C, indicating a broad temperature adaptability that is uncommon among known thermostable enzymes. The efficient PPi-hydrolyzing capability under both moderate and high temperatures effectively alleviates thermodynamic inhibition in biosynthetic systems. These properties highlight the significant potential of PPase_Tba and PPase_Tar in industrial biocatalysis, molecular diagnostics, and RNA-based biotechnology, presenting broad prospects for applications in biomedical research and biomanufacturing.

PMID:42165196 | DOI:10.1002/cbic.202500892