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Kinetic and structural studies on thermal inactivation of lipoxygenase L1: effect of nonionic surfactants.

Sonati, Srinivasulu and Appu Rao, A. G. (1996) Kinetic and structural studies on thermal inactivation of lipoxygenase L1: effect of nonionic surfactants. Journal of Agricultural and Food Chemistry, 44 (11). 3489-3493, 27 ref..

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Abstract

Lipoxygenase 1 (LOX1) from soybean was irreversibly inactivated at 54C (pH 9.0), the midpoint of the thermal inactivation temp. (Tm) being 44 1C. The kinetics of thermal inactivation of the enzyme followed the first-order kinetics with an estimated rate constant of 1.5 x 10-4 s-1 and a half-life of 36 min at 42C. Irreversible inactivation of the enzyme involved oxidation of cysteine residues resulting in intermolecular cross-linking. The conformation of the enzyme molecule remained practically unaltered. The nonionic surfactants Brij 35 and Tween 20 enhanced thermal stability. Enhanced thermal stability could be due to strengthening of hydrophobic interactions around cysteine residues.

Item Type: Article
Uncontrolled Keywords: ENZYMES-; LIPOXYGENASES-; PHYSICAL-PROPERTIES; SEEDS-; SOYBEANS-; THERMOPHYSICAL-PROPERTIES; VEGETABLES-SPECIFIC; THERMAL-STABILITY
Subjects: 600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 07 Aug 2008 11:54
Last Modified: 28 Dec 2011 10:01
URI: http://ir.cftri.com/id/eprint/7820

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