The biocatalysis of purified soybean lipoxygenase (LOX) (EC 1.13.11.12) using linoleic acid as a substrate model was investigated in selected organic solvent media, including chloroform, dichloromethane, hexane, iso-octane, octane and toluene. The results indicated that there was a 2.6 fold increase in LOX activity in the monophasic iso-octane medium compared to that obtained in the aqueous medium. In addition, the optimum concentration of octane and iso-octane in the biphasic medium containing the organic solvent and Tris-HCl buffer solution, was determined to be 3.5 and 4%, respectively, for LOX activity which resulted in a further increase in LOX activity. The immobilized LOX showed better substrate specificity towards linoleic acid, followed by arachidonic acid. The enzymatically-catalyzed end-products were investigated, and the results indicated that different proportions of the 9- and 13-HPOD isomers were produced by LOX biocatalysis depending on the reaction medium used and the free or immobilized state of the enzyme. (Abstract shortened by UMI.)
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.30368 |
Date | January 2000 |
Creators | Dioum, Ndeye. |
Contributors | Kermasha, Selim (advisor) |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Master of Science (Department of Food Science and Agricultural Chemistry.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 001744373, proquestno: MQ64344, Theses scanned by UMI/ProQuest. |
Page generated in 0.0074 seconds