Related Experiment Video
Updated: Jun 10, 2026
Lignin Down-regulation of Zea mays via dsRNAi and Klason Lignin Analysis
Published on: July 23, 2014
Recombinant maize 9-lipoxygenase: expression, purification, and properties
E V Osipova1, I R Chechetkin, Y V Gogolev
1Kazan Institute of Biochemistry and Biophysics, Kazan Research Center, Russian Academy of Sciences, Russia.
Abstract:
Expression of maize 9-lipoxygenase was performed and optimized in Escherichia coli Rosetta(DE3)pLysS. The purity of recombinant protein obtained during Q-Sepharose and Octyl-Sepharose chromatographies in an LP system at 4 degrees C was >95%. Maximum activity of the lipoxygenase reaction was observed at pH 7.5. Enzyme stability was studied at pH 4.5 to 9.5 and in the presence of different compounds: phenylmethanesulfonyl fluoride, beta-mercaptoethanol, ammonium sulfate, and glycerol. HPLC and GC-MS analysis showed that enzyme produced 99% 9S-hydroperoxide from linoleic acid. 13-Hydroperoxide (less than 1%) consisted of S- and R-enantiomers in ratio 2 : 3.
