Lipoxygenase isoenzymes of french bean pericarp: Separation, characterization and chlorophyll-bleaching activity

Two lipoxygenase isoenzymes, Lα and Lβ, were partially purified from pericarp of french bean. The two isoenzymes differed in pI, M r , apparent K M , and lag phase. Both could be categorized as type 2 lipoxygenase, based on their acidic optimum pH, simultaneous production of carbonyl compounds and h...

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Published inPhytochemistry (Oxford) Vol. 28; no. 4; pp. 1019 - 1024
Main Authors Abbas, Jawad, Rouet-Mayer, Marie-Aude, Lauriere, Chrstiane
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 1989
Elsevier
Subjects
Analytical, structural and metabolic biochemistry
Biological and medical sciences
chlorophyll-bleaching
chromatofocusing
Enzymes and enzyme inhibitors
french bean
Fundamental and applied biological sciences. Psychology
Leguminosae
lipoxygenase isoenzymes
Oxidoreductases
Phaseolus vulgaris
french bean
lipoxygenase isoenzymes
chromatofocusing
Leguminosae
Phaseolus vulgaris
chlorophyll-bleaching
Vegetals
Purification
Enzyme
Isozyme
Dicotyledones
Angiospermae
Spermatophyta
Lipoxygenase
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Summary:Two lipoxygenase isoenzymes, Lα and Lβ, were partially purified from pericarp of french bean. The two isoenzymes differed in pI, M r , apparent K M , and lag phase. Both could be categorized as type 2 lipoxygenase, based on their acidic optimum pH, simultaneous production of carbonyl compounds and hydroperoxides in the presence of oxygen, aerobic chlorophyll-bleaching activity and inhibition by chlorophyll a. In the presence of a sufficient amount of preformed hydroperoxides, it was possible to show competitive inhibition of Lα and Lβ by chlorophyll a.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0031-9422
1873-3700
DOI:10.1016/0031-9422(89)80175-X