Identification and characterization of a novel phthalate-degrading hydrolase from a soil metagenomic library

Phthalate esters have raised public concerns owing to their effects on the environment and human health. We identified a novel phthalate-degrading hydrolase, EstJ6, from a metagenomic library using function-driven screening. Phylogenetic analysis indicated that EstJ6 is a member of family IV esterases. EstJ6 hydrolyzed various dialkyl and monoalkyl phthalate esters, and exhibited high hydrolytic activity (128 U/mg) toward dibutyl phthalate at 40 °C and pH 7.5. EstJ6 hydrolyzed not only common phthalate esters with simple side chains but also diethylhexyl phthalate and monoethylhexyl phthalate, which have complex and long side chains. Site-directed mutagenesis indicated that the catalytic triad residues of EstJ6 consists of Ser146, Glu240, and His270. EstJ6 is therefore a promising biodegradation enzyme, and our study illustrates the advantages of a metagenomic approach in identifying enzyme-coding genes for agricultural, food, and biotechnological applications. [Display omitted] •The first reported a novel phthalate esters hydrolase from a metagenomic library.•Phthalate-degrading hydrolase (EstJ6) belonged to a new member in family IV.•EstJ6 could hydrolyze various dialkyl Phthalate esters (PAEs) and monoalkyl PAEs.•EstJ6 could hydrolyze DEHP and MEHP with long and complex side chains.