Hydrolyzes phenolic esters, such as phenyl acetate, nitrophenyl acetate and naphtyl acetate (PubMed:1368608, PubMed:7704276, PubMed:9571805, PubMed:15803517). Can act on a wide range of esters, but reaction rate and enantioselectivity differ significantly depending on the substrate (PubMed:1368608, PubMed:9571805). Shows a preference for esters with small acyl groups (PubMed:15213385). Also shows low perhydrolase activity, and catalyzes the reversible formation of peroxycarboxylic acids from carboxylic acids and hydrogen peroxide (PubMed:15803517, PubMed:20112920, PubMed:22618813). In vitro, enzyme-generated peracetic acid oxidizes bromide ion to bromonium, which reacts with monochlorodimedone to form bromochlorodimedone (PubMed:7704276, PubMed:20112920, PubMed:22618813). a phenyl acetate + H2O = a phenol + acetate + H(+) H2O + peracetic acid = acetate + H(+) + H2O2 a percarboxylic acid + H2O = a carboxylate + H(+) + H2O2 kcat is 9 sec(-1) with ethyl acetate as substrate. kcat is 25 sec(-1) with methyl acetate as substrate. kcat is 100 sec(-1) with peracetic acid as substrate. kcat is 0.12 sec(-1) with acetic acid as substrate. kcat is 0.094 sec(-1) with hydrogen peroxide as substrate (PubMed:20112920). kcat is 15 sec(-1) with methyl acetate as substrate (PubMed:22618813). Optimum pH is above 9.0 for esterase activity. Optimum temperature is 70 degrees Celsius for esterase activity. Dimer of trimers. It is unlikely that perhydrolysis is the natural function of perhydrolases. Instead, perhydrolysis is probably an accidental (promiscuous) activity (Probable). Perhydrolysis is an important reaction that makes peroxycarboxylic acids, which are useful oxidants in organic chemistry, for lignin removal and pulp bleaching and for disinfecting wastewater and disinfecting equipment for food and medical applications (PubMed:23325572). Perhydrolases were previously known as metal-free haloperoxidases (Probable). Belongs to the AB hydrolase superfamily. Bacterial non-heme haloperoxidase / perhydrolase family.