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Structure and kinetic thermal stability studies of the interaction of monohydric alcohols with lipoxygenase 1 from soybeans (Glycine max).

Sonati, Srinivasulu and Appu Rao, A. G. (1995) Structure and kinetic thermal stability studies of the interaction of monohydric alcohols with lipoxygenase 1 from soybeans (Glycine max). Journal of Agricultural and Food Chemistry, 43 (3). pp. 562-567.

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Abstract

Effects of monohydric alcohols on properties of soybean lipoxygenase 1 (EC 1.13.11.12; LOX1) were investigated. Monohydric alcohols inhibited LOX1 activity; inhibition was reversible and of mixed type. Monohydric alcohols also increased Km and decreased Vmax. At very low concn. of alcohols, no structural changes were observed in the enzyme molecule, implying that the inhibition by monohydric alcohols could be due to the binding of alcohols at the substrate binding/catalytic site. Monohydric alcohols at higher concn. induced more ordered structure in the enzyme. The equilibrium constants obtained for native to helical intermediate(s) transitions are in the millimolar range and increased with the C chain length of alcohols. Free energy changes for the transitions were small but positive in nature. The environment around aromatic amino acid residues became more hydrophobic in alcohols. Alcohols decreased the thermal stability of LOX1. Activational enthalpy and activational entropy of thermal inactivation increased in the presence of alcohols. [From En summ.]

Item Type: Article
Uncontrolled Keywords: ALCOHOLS-; ENZYMES-; LIPOXYGENASES-; SEEDS-; SOYBEANS-; VEGETABLES-SPECIFIC
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 May 2012 09:23
Last Modified: 08 May 2012 09:23
URI: http://ir.cftri.com/id/eprint/7883

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