Affiliations 

  • 1 Laboratory of Enzyme Engineering, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China
  • 2 Department of Chemical and Environmental Engineering, Faculty of Science and Engineering, University of Nottingham Malaysia, Jalan Broga, 43500 Semenyih, Selangor Darul Ehsan, Malaysia
  • 3 Laboratory of Enzyme Engineering, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China. Electronic address: fmb@njau.edu.cn
J Biosci Bioeng, 2020 Mar;129(3):327-332.
PMID: 31585857 DOI: 10.1016/j.jbiosc.2019.09.006

Abstract

In this study, the bacterial lipoxygenase (LOX) gene from Pseudomonas aeruginosa ATCC27853 (pse-LOX) was cloned, sequenced and heterologous expressed in Escherichia coli by auto-induction expression strategy. Production of the recombinant pse-LOX (pse-rLOX) gene up to 23,850 U/mL (264 mg pure protein/L bacterial culture fluid) was observed in the end of this process. To the best of our knowledge, this is the first attempt to manipulate LOX heterologous expression process using auto-induction expression approach, and it is the highest production of recombinant LOX compared with other reports. Subsequently, the resulted pse-rLOX was proved to efficiently degrade triphenylmethane dyes such as malachite green, brilliant green and aniline blue. Generally, an overproduction of the LOX from P. aeruginosa was observed in E. coli, and this recombinant gene is a potential candidate as biocatalyst for triphenylmethane dyes decolorization.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.