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Inhibition of lipoxygenase 1 by phosphatidylcholine micelles-bound curcumin.

Began, G and Sudharshan, E and Appu Rao, A. G. (1998) Inhibition of lipoxygenase 1 by phosphatidylcholine micelles-bound curcumin. Lipids, 33 (12). pp. 1223-8. ISSN 0024-4201

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Abstract

Curcumin (diferuloyl methane) from rhizomes of Curcuma longa L. binds to phosphatidylcholine (PC) micelles. The binding of curcumin with PC micelles was followed by fluorescence measurements. Curcumin emits at 490 nm with an excitation wavelength of 451 nm after binding to PC-mixed micelles stabilized with deoxycholate. Curcumin in aqueous solution does not inhibit dioxygenation of fatty acids by Lipoxygenase 1 (LOX1). But, when bound to PC micelles, it inhibits the oxidation of fatty acids. The present study has shown that 8.6 microM of curcumin bound to the PC micelles is required for 50% inhibition of linoleic acid peroxidation. Lineweaver-Burk plot analysis has indicated that curcumin is a competitive inhibitor of LOX1 with Ki of 1.7 microM for linoleic and 4.3 microM for arachidonic acids, respectively. Based on spectroscopic measurements, we conclude that the inhibition of LOX1 activity by curcumin can be due to binding to active center iron and curcumin after binding to the PC micelles acts as an inhibitor of LOX1.

Item Type: Article
Uncontrolled Keywords: Curcumin phenolic antioxidants LOX1
Subjects: 600 Technology > 08 Food technology > 30 Spices/Condiments
600 Technology > 08 Food technology > 32 Antioxidants
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 01 Jul 2009 11:12
Last Modified: 28 Dec 2011 09:39
URI: http://ir.cftri.com/id/eprint/2200

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