Catalyzes the removal of the phthalyl group from phthalyl amides generating phthalate and an amine. The enzyme has a broad substrate specificity and hydrolyzes phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines; substitutions allowed on the phthalyl group include 6-F, 6-NH(2), 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. a phtalamide + H2O = a primary amine + phthalate Inhibited by iodoacetate, p-hydroxymercuric benzoate and copper ions. Optimum pH is 7.8-8.4. Optimum temperature is 28-34 degrees Celsius. Monomer. The N-terminus is blocked. The broad substrate acceptance, high catalytic activity, and stability at high salt or substrate concentration of the enzyme indicates that it can serve as a gentle method for deprotecting phthalimido and o-phthalyl protected amides in new chemo-enzymatic synthetic routes.