Esterase likely involved in ester/lipid metabolism. Shows strong substrate selectivity toward short, straight chain alkyl esters with the highest activity toward four atom chains. The physiological substrate is unknown (PubMed:25354081). Is able to hydrolyze ester bonds within a wide range of p-nitrophenyl derivatives (C2-C14) in vitro (PubMed:20957207). a carboxylic ester + H2O = a carboxylate + an alcohol + H(+) a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+) an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+) a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl hexanoate. Optimum temperature is 39 degrees Celsius for the hydrolysis of p-nitrophenyl hexanoate. Monomer. Contains two distinct structural domains: an almost globular alpha/beta fold domain and an inserted cap domain which interacts with the alpha/beta fold domain. Belongs to the AB hydrolase superfamily.