The gene encoding a novel acidic lipoxygenase from Myxococcus xanthus DK1622 (accession: WP_011551853.1) was cloned into vector pET-28a and expressed in Escherichia coli BL21(DE3). The recombinant enzyme (rMxLOX), with a molecular weight of approximately 80 kDa, was purified to homogeneity using one-step nickel-affinity chromatography and showed an activity of 5.6 x 10(4) U/mg. The optimum pH and temperature for rMxLOX activity were found to be 3.0 and 30 degrees C, respectively. Purified rMxLOX exhibited activity towards linoleic acid and arachidonic acid as substrates, with linoleic acid being the better substrate (K-m and K-cat values of 0.048 mM and 13.3/s, respectively). The synthetic dye aniline blue was decolorized 69.7 +/- 3.5%, following incubation with rMxLOX for 35 min. These results reveal the potential for the use of rMxLOX in the pulp, textile, and wastewater treatment industries. (c) 2017 Elsevier Inc. All rights reserved.