Degradation of 3-chloropropionic acid (3CP) byPseudomonas sp. B6P isolated from a rice paddy field

Abstract

A bacterium that degrades 3-chloropropionic acid (3CP) was isolated from local paddy (rice) agricultural soil by enrichment culture. Taxonomic analysis identified the strain as Pseudomonas sp. Strain-mediated degradation of 3CP released chloride ions into the growth medium, and the degradation of ~100% of 20 mM 3CP was monitored by high performance liquid chromatography (HPLC). The putative Pseudomonas sp. dehalogenase that released the chloride ions from 3CP was induced by growth of the bacterium in the presence of 3CP as the sole carbon source. The dehalogenase showed activity against a specific type of halogenated aliphatic acids, and the highest activity was obtained with 3CP. However, the enzyme could only remove halogen atoms from 3-carbon alkanoic acids if the halogen was at the β-but not the -position. In crude bacterial extracts, the dehalogenase activity with 3CP was maximum at 30 °C, over a broad pH range (pH 7.5 optimum) and had an apparent K ms of 0.25 ± 0.04 mM and 0.67 ± 0.17 mM for 3CP and 2,3-dichloropropionic acid, respectively.

Molecular Modelling and Functional Studies of the Non-Stereospecific α-Haloalkanoic Acid Dehalogenase (DehE) fromRhizobiumSP. RC1 and its Association with 3-Chloropropionic Acid (β-Chlorinated Aliphatic Acid)

“…Haloalkanoic acid dehalogenase has also been widely confirmed to act on α-halogenated carboxylic acid compounds but not on β-halogenated carboxylic acids. Dehalogenation of β-halogenated carboxylic acids, such as 3-chloropropionate (3CP), is not well studied, and its mechanism is far from clear (27,50,51).…”

Enhancement of haloacetate dehalogenase production by strain mutation and condition optimization

“…However, the microorganism was unable to grow in 3-CPS as a sole carbon source. Since the reported chloroacetate dehalogenase enzymes showed no activity with 3-CPS, and 3-chloropropionate dehalogenases have no activity with CAS [12,15,16], the chloroacetate dehalogenase presented in this study may be a novel enzyme.…”

Molecular Characterization of Monochloroacetate-DegradingArthrobactersp. Strain D2 Isolated from Universiti Teknologi Malaysia Agricultural Area

“…D2 was isolated, and the partial dehalogenase sequence of the novel DehD2 involved in the dehalogenation of MCA, MBA, 2,2DCP, and D,L2CP, and nonstereoselective dehalogenation of D-2CP and L-2CP was characterized. Information on substrate specificity will provide some idea to alter amino acid residues and obtain enzyme-substrate specificities, especially studies on β-halocarboxylic acid (βHA) degradation, for example, 3CP (Mesri, Wahab, and Huyop 2009). Computational analysis of DehE provides a basic idea that key catalytic residues are able to bind to 3CP similarly to that of D-or L-2CP (Hamid et al 2013).…”