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Isolation, purification and characterization of lipoxygenase isozymes from canola (Brassica napus cv, Westar) seed

Lipoxygenase was extracted from Canola seeds (Brassica napus cv, Westar) and partially purified by precipitated with ammonium sulfate at 20-50% of saturation. The optimum pH for the enzyme activity was 7.5 and its K$ sb{ rm m}$ value was 2.0 $ times$ 10$ sp{-4}$ M. The activity of the enzyme extract was considerably greater on linoleic acid than on its ester or on linolenic acid. The effect of cyanide on the enzyme activity was also investigated. / Further purification of the enzyme extract was performed by successive chromatography on ion-exchange and gel filtration, using FPLC system. Four lipoxygenase isozymes (I, IIA, IIB and III) were separated. The homogeneity of each isozyme was demonstrated by the presence of a single protein band on SDS-PAGE gel electophoresis. The molecular weights of isozymes I, IIA, IIB and III were, respectively, 72,000, 106,000, 78,000 and 62,000. The optimum pH for lipoxygenase activity was 6.5 for isozyme I and 6.0 for isozymes IIA, IIB and III.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.59272
Date January 1990
CreatorsKhalyfa, Abdelnaby
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Department of Food Science and Agricultural Chemistry.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001070991, proquestno: AAIMM63471, Theses scanned by UMI/ProQuest.

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