2012
DOI: 10.1007/s00253-012-4457-6
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Overproduction, purification, and characterization of extracellular lipoxygenase of Pseudomonas aeruginosa in Escherichia coli

Abstract: Lipoxygenase (LOX; EC 1.13.11.12,) is an enzyme that is widely used in food industry to improve aroma, rheological, or baking properties of foods. In this study, we described the expression and characterization of Pseudomonas aeruginosa LOX in Escherichia coli. The recombinant LOX was successfully expressed and secreted by E. coli using its endogenous signal peptide. When induced with 1 mM isopropyl β-D-1-thiogalactopyranoside (final concentration) at 20 °C for 47 h, the titer of the recombinant enzyme reached… Show more

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Cited by 36 publications
(48 citation statements)
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“…oxygenates different fatty acids with variable specificity [69]. Linoleic acid is converted by the secretable P. aeruginosa LOX [64] almost exclusively to 13S-HpODE [70] and a similar product specificity was reported for two LOX-isoforms from Nostoc punctiforme [65]. LOXs in lower organisms occasionally occur as fusion proteins combining different catalytic activities within one protein.…”
Section: Properties Structures and Biological Function Of Bacterial mentioning
confidence: 64%
“…oxygenates different fatty acids with variable specificity [69]. Linoleic acid is converted by the secretable P. aeruginosa LOX [64] almost exclusively to 13S-HpODE [70] and a similar product specificity was reported for two LOX-isoforms from Nostoc punctiforme [65]. LOXs in lower organisms occasionally occur as fusion proteins combining different catalytic activities within one protein.…”
Section: Properties Structures and Biological Function Of Bacterial mentioning
confidence: 64%
“…Several bacterial LOXs have been successfully expressed in prokaryotes. As claimed by Lu et al (Lu et al, 2013) the highest level of expressed LOX so far is 3.89 U/ml and has been achieved by expressing P. aeruginosa LOX in E. coli. Most heterologous production of LOXs in E. coli is performed at temperatures ranging from 8 to 20 C. This low temperature can cause additional production costs in upscaling the production process due to the cooling energy that is required for fermenters during growth of the expression host.…”
Section: Expression and Production Of Lox In Microbial Hostsmentioning
confidence: 87%
“…P. aeruginosa, a facultative human pathogen, expresses psaALOX1 as secreted protein (the native protein carries a secretion signal peptide) but its biological role has not been studied in detail. The enzyme can be expressed as recombinant non-secreted protein at high levels (more than 5 mg purified protein per 50 ml liquid culture) in E. coli and its proteinchemical and enzymatic properties have been characterized [26,28]. It has been crystallized and the X-ray structure was solved to a resolution of 1.7-2.1 Å [29].…”
Section: Bacterial Lox Genes and Lox-isoformsmentioning
confidence: 99%
“…The most comprehensively characterized bacterial LOX-isoform is that from Pseudomonas aeruginosa [25][26][27]. This enzyme (psaALOX1) oxygenates arachidonic acid to 15S-HpETE and thus must be classified as arachidonic acid 15-LOX.…”
Section: Bacterial Lox Genes and Lox-isoformsmentioning
confidence: 99%