Abstract
A cold-active phthalate esters hydrolase gene (designated dphB) was identified through functional screening of a metagenomic library derived from biofilms of a wastewater treatment plant. The enzyme specifically catalyzed the hydrolysis of dipropyl phthalate, dibutyl phthalate, and dipentyl phthalate to the corresponding monoalkyl phthalate esters at low temperatures. The catalytic triad residues of DphB were proposed to be Ser159, Asp251, and His281.
Highlights
Phthalate esters (PEs) are a category of toxic organic compounds that wildly used as additives or plasticizers in the manufacture of plastics [1]
Subclone Library Production and Screening Fosmid DNA of selected colonies was isolated as templates by the large-construct kit (QIAGEN) and the specific polymerase chain reaction (PCR) amplifications of the reported DBP hydrolase gene [15] were first performed by the primers P1 (59ATG AAC GAC GGC GCC ACT CGT TAT-39) and P2 (59TCA TGC TGC GCC GTT AGC TTC GGC-39)
The substrate specificity of the recombinant DphB was investigated with C1–C7 chain dialkyl PEs (dimethyl phthalate (DMP), diethyl phthalate (DEP), dipropyl phthalate (DPrP), DBP, dipentyl phthalate (DPP), dihexyl phthalate (DHP), and diheptyl phthalate (DHpP)) and monoalkyl
Summary
Phthalate esters (PEs) are a category of toxic organic compounds that wildly used as additives or plasticizers (softeners) in the manufacture of plastics [1]. This enzyme displayed specific dialkyl PEs hydrolase activity toward three esters, commonly used in the plastic industry, dipropyl phthalate (DPrP), DBP, and dipentyl phthalate (DPP) at low temperatures, with an optimum temperature of 10uC.
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