Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.)

Lorenzi, Vannina; Maury, Jacques; Casanova, Javier Carrera; Berti, Liliane

doi:10.1016/j.plaphy.2006.09.001

Cited by 40 publications

(45 citation statements)

References 24 publications

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“…Linolenic and linoleic acids are the most common plant substrates for LOXs (Siedow, 1991), and linoleic acid is particularly important as a substrate (Lorenzi et al, 2006). A comparison of the substrate specificity of the six Arabidopsis LOXs revealed that the 9-LOXs AtLOX1 and AtLOX5 oxygenate linoleic acid and linolenic acid rather than arachidonic acid (Bannenberg et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

The Pepper 9-Lipoxygenase GeneCaLOX1Functions in Defense and Cell Death Responses to Microbial Pathogens

2009

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Lipoxygenases (LOXs) are crucial for lipid peroxidation processes during plant defense responses to pathogen infection. A pepper (Capsicum annuum) 9-LOX gene, CaLOX1, which encodes a 9-specific lipoxygenase, was isolated from pepper leaves. Recombinant CaLOX1 protein expressed in Escherichia coli catalyzed the hydroperoxidation of linoleic acid, with a K m value of 113. 9 mM. Expression of CaLOX1 was differentially induced in pepper leaves not only during Xanthomonas campestris pv vesicatoria (Xcv) infection but also after exposure to abiotic elicitors. Transient expression of CaLOX1 in pepper leaves induced the cell death phenotype and defense responses. CaLOX1-silenced pepper plants were more susceptible to Xcv and Colletotrichum coccodes infection, which was accompanied by reduced expression of defense-related genes, lowered lipid peroxidation, as well as decreased reactive oxygen species and lowered salicylic acid accumulation. Infection with Xcv, especially in an incompatible interaction, rapidly stimulated LOX activity in unsilenced, but not CaLOX1-silenced, pepper leaves. Furthermore, overexpression of CaLOX1 in Arabidopsis (Arabidopsis thaliana) conferred enhanced resistance to Pseudomonas syringae pv tomato, Hyaloperonospora arabidopsidis, and Alternaria brassicicola. In contrast, mutation of the Arabidopsis CaLOX1 ortholog AtLOX1 significantly increased susceptibility to these three pathogens. Together, these results suggest that CaLOX1 and AtLOX1 positively regulate defense and cell death responses to microbial pathogens.

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Section: Discussionmentioning

confidence: 99%

The Pepper 9-Lipoxygenase GeneCaLOX1Functions in Defense and Cell Death Responses to Microbial Pathogens

2009

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“…LOX enzyme from pea seeds was purified 47.2-fold (Szymanowska et al, 2009). Lorenzi et al (2006) obtained 65-fold purification of LOX from olives using differential centrifugation and hydrophobic chromatography. Three isoenzymes of LOX from pearl millet seedlings were purified using ammonium sulfate fractionation, DEAE-Sephadex A-50, and Sephadex G-200 gel-filtration (about 46.5-, 73.6-, and 115.7-fold, respectively) (Babitha et al, 2004).…”

Section: Lox Activity During Germination Of Poppy Seeds and Enzyme Pumentioning

confidence: 99%

“…Most plant LOX have a relative molecular mass ranging from 94 to 104 kDa (Siedow, 1991). The relative molecular mass of LOX from olive fruit is 98 kDa (Lorenzi et al, 2006), and LOX from pea seeds is 93 kDa (Szymanowska et al, 2009). However, several publications reported relative molecular masses of 85 kDa for LOX purified from banana leaves (Kuo et al, 2006) and 74 kDa for LOX from chicory (Daglia et al, 2005).…”

Section: Lox Activity During Germination Of Poppy Seeds and Enzyme Pumentioning

confidence: 99%

“…The K m value of LOX from pea seeds was 0.44 mM (Szymanowska et al, 2009) and was 0.15 mM in LOX purified from banana leaves (Kuo et al, 2006) and soluble LOX from chicory (Daglia et al, 2005). Other plant LOXs display K m values in the lower micromolar range (Fornaroli et al, 1999;Lorenzi et al, 2006;Sellhorn et al, 2011).…”

Section: Kinetic Study and The Effect Of Calcium Ion Concentration Onmentioning

confidence: 99%

“…The major product reported, for other plant LOXs such as soluble LOX purified from tomato fruits, was 9-HPODE (96%), while only 1% 13-HPODE was formed (Suurmeijer et al, 1998); olive LOX converted linoleic acid only to 13-HPODE (Lorenzi et al, 2006); and LOX from developing rice seedlings had dual positional specificity, releasing both C-13 and C-9 oxidized products (Wang et al, 2008). The 9-or 13-selective positional specificity of LOXs allows for production of specific metabolites with diverse roles in plant growth, development, or defense.…”

Section: Characterization Of Lox Reaction Productsmentioning

confidence: 99%

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Purification and properties of lipoxygenase from opium poppy seedlings(Papaver somniferum L.)

Holková¹,

Bilka²,

Rauová³

et al. 2016

Turk J Biol

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Lipoxygenase (linoleate:oxygen oxidoreductase; EC 1.13.11.12; LOX) is a key enzyme in the signaling pathway leading to the production of biologically active compounds involved in plant growth development and stress responses. In this study the novel LOX enzyme from opium poppy (Papaver somniferum L.) seedlings was purified to electrophoretic homogeneity and characterized. LOX activity during the germination of opium poppy seeds was analyzed, and the highest LOX activity was determined on the fourth day of germination. Opium poppy LOX was purified from 4-day-old poppy seedlings after ammonium sulfate precipitation followed by hydrophobic chromatography (Phenyl-Sepharose CL-4B), ion exchange chromatography (Q-Sepharose), and affinity chromatography (linoleyl-aminopropyl agarose) for the first time. The relative molecular weight of purified LOX was estimated to be 78 kDa by immunoblotting. The highest enzyme activity occurred at pH 6.5 and 0.75 mM calcium ion concentration. LOX showed preferential activity towards linoleic acid followed by linolenic acid as a substrate. To investigate the positional specificity of the LOX reaction, purified LOX was incubated with linoleic acid, and the products were analyzed by high-performance liquid chromatography. Opium poppy LOX converted linoleic acid to 13-hydroperoxy-(9Z,11E)-octadecadienoic acid (63.5%) and, to a lesser extent, 9-hydroperoxy-(10E,12Z)-octadecadienoic acid (36.5%).

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Enzymes in Quality and Processing of Tropical and Subtropical Fruits

Liavoga

Matella²

2012

Tropical and Subtropical Fruits

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Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.)

Cited by 40 publications

References 24 publications

The Pepper 9-Lipoxygenase GeneCaLOX1Functions in Defense and Cell Death Responses to Microbial Pathogens

The Pepper 9-Lipoxygenase GeneCaLOX1Functions in Defense and Cell Death Responses to Microbial Pathogens

Purification and properties of lipoxygenase from opium poppy seedlings(Papaver somniferum L.)

Enzymes in Quality and Processing of Tropical and Subtropical Fruits

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