Biodegradation of phthalic acid esters (PAEs) by Bacillus sp. LUNF1 and characterization of a novel hydrolase capable of catalyzing PAEs

Identification and characterisation of moderately thermostable diisobutyl phthalate degrading esterase from a Great Artesian Basin Bacillus velezensis NP05

“…8 A.). The study by Fan, Li [52] research group showed similar results in modelling. The dphBL1 esterase is capable of degrading Dibutyl phthalate (DBP), Diethyl phthalate (DEP), and Benzyl butyl phthalate (BBP).…”

“…EMBOSS needle pairwise analysis of Bacillus sp. LUNF1 (dphBL1) [52] , to this studies pnbA shows a 99.6 % similarity based on the sequence alignment. A total of 8 amino acids are different at various positions in comparison of pnbA to dphBL1 (see supplementary material).…”

“…However, they only report hydrolysis to mono-form phthalate and not complete hydrolysis to PTH. The pnbA esterase from this study seems to be able to degrade more DIBP (83 %) than dphBL1 can degrade DBP (64.7 %), DEP (65.0 %), or BBP (46.2 %) under ideal conditions from a rudimentary perspective [52] . The dphBL1 esterase exhibits broader pH activity from 6 to 9 and an optimum temperature of 40 °C.…”

“…They did not ascertain the thermostability of dphBL1, so it is not known if dphBL1 is thermostable. However, given the optimum activity for pnbA in this study is 55 °C and the dphBL1 esterase is 40 °C [52] , it is tenable to say pnbA has a higher thermostability. This is weakly supported by the fact that pnbA has one more alanine residue than dphBL1.…”

“…Although not novel it should not be overlooked as it has demonstrated novel phthalate and plastic degrading capabilities. There are a handful of studies of Bacillus genera phthalate degrading esterases [ 20 , 23 , 24 , 52 ]. A study by Ding, Wang [20] reported a CarEW capable of two-step hydrolysis of DIBP to MIBP and PTH.…”