کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5515996 | 1542303 | 2017 | 5 صفحه PDF | دانلود رایگان |

- Cloning and functional expression of a lipoxygenase gene from Myxococcus xanthus in Escherichia coli.
- rMxLOX showed its maximum activity at pH 3.0, differing significantly from LOXs from other sources.
- rMxLOX can efficiently degrade methyl blue and aniline blue.
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 Ã 104 U/mg. The optimum pH and temperature for rMxLOX activity were found to be 3.0 and 30 °C, respectively. Purified rMxLOX exhibited activity towards linoleic acid and arachidonic acid as substrates, with linoleic acid being the better substrate (Km and kcat 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.
Journal: Protein Expression and Purification - Volume 138, October 2017, Pages 13-17