Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea)
Shaban, N., Sadek, O., Serag, E., Malki, A. (2018). Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea). EKB Journal Management System, 14(1), 270-285. doi: 10.21608/blj.2018.285170
Nadia Z. Shaban; Omayma M. Sadek; Eman A, Serag; Ahmed M. Malki. "Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea)". EKB Journal Management System, 14, 1, 2018, 270-285. doi: 10.21608/blj.2018.285170
Shaban, N., Sadek, O., Serag, E., Malki, A. (2018). 'Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea)', EKB Journal Management System, 14(1), pp. 270-285. doi: 10.21608/blj.2018.285170
Shaban, N., Sadek, O., Serag, E., Malki, A. Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea). EKB Journal Management System, 2018; 14(1): 270-285. doi: 10.21608/blj.2018.285170

Purification, characterization and kinetic properties of partially purified lipoxygenase, extracted from peanut seeds (Arachis hypogaea)

Biochemistry Letters
Volume 14, Issue 1, 2018, Page 270-285  XML PDF (711.38 K)
DOI: 10.21608/blj.2018.285170
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Authors
Nadia Z. Shaban; Omayma M. Sadek; Eman A, Serag; Ahmed M. Malki
Biochemistry department, Faculty of Science, Alexandria University, Egypt.
Abstract
Background: Lipoxygenases (LOX) are found widely in plants, fungi and animals. These enzymes catalyze the hydroperoxidation of polyunsaturated fatty acids containing cis, cis-1,4-pentadiene moieties. Furthermore, plants contain multiple isoforms of the LOX enzyme which differs in their biochemical properties. Objectives: The present study was carried out to isolate, purify and characterize LOX from peanut seeds. Methods: The concentrated dialyzed cell free extract was fractionated using ammonium sulfate followed by ion exchange chromatography using DEAE-cellulose. SDS-PAGE was performed for the molecular weight determination. Results: Purification of peanut LOX indicates that peanut LOX has three isoenzymes with molecular masses: 113, 113 and 95 KD. The isoenzymes exhibited optimum pH of LOX- 1 and 2 at pH 6 while the optimum pH of LOX -3 was at pH 8. While, the three isoenzymes have the same optimum temperature; 20ᴼC. The Vmax and the Km values of the three isoenzymes were estimated. Our data showed that the LOX activity was irreversibly inhibited by a-chymotrypsin to about 66% as compared to the control. While, atropine had no effect on LOX activity. The heating of peanut at 80ᴼC for 2 and 10 min and at 90ᴼC for 2 min inhibited the LOX activity by about 71.4 %, 84 % and 90.8 %, respectively.  While, the heating of peanut at 80ᴼC for 10 min extend the shelf- life of peanut.                                                                                                                                        2018 Publisher All rights reserved.
Keywords
Lipoxygenases isoenzymes; peanut; -chymotrypsin; atropine
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