Zhang_2023_J.Hazard.Mater_463_132847

Prolonged and widespread use of pyrethroid pesticides a significant concern for human health. The initial step in pyrethroid bioremediation involves the hydrolysis of ester-bond. In the present study, the esterase genes est10 and est13, derived from Bacillus subtilis, were successfully cloned and expressed in Escherichia coli. Recombinant Est10 and Est13 were classified within esterase families VII and XIII, respectively, both of which exhibited conserved G-X-G-X-G motifs. These enzymes demonstrated the capability to degrade pyrethroids, with Est13 exhibiting superior efficiency, and thus was selected for further investigation. The degradation products of beta-cypermethrin by Est13 were identified as 3-phenoxybenzoic acid, 3-phenoxybenzaldehyde, and 3-(2,2-Dichloroethenyl)- 2,2-dimethyl-cyclopropanecarboxylate, with key catalytic triads comprising Ser(93), Asp(192), and His(222). Notably, Est13 exhibited the highest beta-cypermethrin-hydrolytic activity at 25 degreesC and a pH of 7.0, showing robust stability in low and medium temperature environment and a broad range of pH levels. Furthermore, Est13 displayed notable resistance to organic solvents and NaCl, coupled with wide substrate specificity. Moreover, Est13 exhibited substantial efficiency in removing beta-cypermethrin residues from various food items such as milk, meat, vegetables, and fruits. These findings underscore the potential of Est13 for application in the bioremediation of pyrethroid-contaminated environments and reduction of pyrethroid residues in food products.