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Expression, purification, and characterization of a novel acidic Lipoxygenase from Myxococcus xanthus.

Authors :
Qian, Hui
Xia, Bingjie
He, Yujun
Lu, Zhaoxin
Bie, Xiaomei
Zhao, Haizhen
Zhang, Chong
Lu, Fengxia
Source :
Protein Expression & Purification. Oct2017, Vol. 138, p13-17. 5p.
Publication Year :
2017

Abstract

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 × 10 4 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 (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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10465928
Volume :
138
Database :
Academic Search Index
Journal :
Protein Expression & Purification
Publication Type :
Academic Journal
Accession number :
124576957
Full Text :
https://doi.org/10.1016/j.pep.2017.05.006