Enzymes belonging to the structural family of CE-7 esterases, such as cephalosporin C deacetylases and acetyl xylan esterases, have recently been shown to have significant activity and selectivity for catalyzing the perhydrolysis of acetyl esters by hydrogen peroxide in aqueous solution, producing peracetic acid in concentrations efficacious for disinfection.  These CE-7 perhydrolases share a conserved structural motif, as well as superior perhydrolysis activity when compared to other α/β-hydrolases.  The wild-type thermophilic perhydrolases isolated from Thermotoga maritima and Thermotoga neapolitana have excellent stability at temperatures of up to 90 °C, making possible a simple and economical purification and isolation process for enzyme production.  Mutants of these two perhydrolases have been produced with significantly improved specific activity and perhydrolytic selectivity when compared to the corresponding wild-type enzymes.  The T. maritima C277S mutant perhydrolase has a 10-fold higher specific activity for perhydrolysis of triacetin than the corresponding wild-type perhydrolase, where selectivity for perhydrolysis of triacetin in aqueous solution is 94 %.