Cloning, expression, purification, and characterization of a thermostable esterase from the archaeon Sulfolobus solfataricus P1

- An esterase gene was isolated from a genomic library of S. solfataricus P1.
- The esterase gene was composed of 942 nucleotides encoding 314 amino acids.
- The enzyme shows remarkable thermal and chemical stability.
- Site-directed mutagenesis revealed a catalytic triad, Ser144-Asp266-His295.
- The enzyme is an archaeal esterase grouped into family V as well as B-type.