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The recombinant L-haloacid dehalogenase from the marine bacterium Psychromonas ingrahamii has been cloned and over-expressed in Escherichia coli. It shows activity towards monobromoacetic (100 %), monochloroacetic acid (62 %), S-chloropropionic acid (42 %), S-bromopropionic acid (31 %), dichloroacetic acid (28 %) and 2-chlorobutyric acid (10 %), respectively. The L-haloacid dehalogenase has highest activity towards substrates with shorter carbon chain lengths (≤ C3), without preference towards a chlorine or bromine at the α-carbon position. Despite being isolated from a psychrophilic bacterium, the enzyme has mesophilic properties with an optimal temperature for activity of 45 °C. It retains above 70 % of its activity after being incubated at 65 °C for 90 min before being assayed at 25 °C. The enzyme is relatively stable in organic solvents as demonstrated by activity and thermal shift analysis. The V max and K m were calculated to be 0.6 μM min(-1) mg(-1) and 1.36 mM with monobromoacetic acid, respectively. This solvent-resistant and stable L-haloacid dehalogenase from P. ingrahamii has potential to be used as a biocatalyst in industrial processes.