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Characterization of horse gram (Dolichos biflorus) lipoxygenase

Characterization of horse gram (Dolichos biflorus) lipoxygenase

Journal of Phytological Research 20(1): 71-79

Lipoxygenases LOX, (EC: 1. 13.12.11) of horse grain (HG) (Dolichos biflorus) was purified to electrophoretic homogeneity and its partial characterization was made using UV CD spectrum. The purification and electrophoretic analysis of horse grain lipoxygenase has revealed that it is a monomeric protein with a molecular mass of 95 5 KDa. This enzyme showed optimum activity at pH 6.8 in between the temperature of 2-5-35 degrees C, and had K-M values for Linolenic and Arachidonic acids as 9.95 and 15.51 mu moles, respectively. This protein on the far UV CD absorption the spectra, showed a negative dip at 208 and 222nm to indicate the presence of alpha-helix and beta strands and near UV CD spectra showed maximum absorption at 278, 282 and 292nm to decide about the contribution of aromatic amino acids towards the tertiary structure of horse grain lipoxygenase. The thermo stability of this protein was observed on increasing the effect of temperature at pH values of 6.8 and 9.0. The inflection point at 40 degrees C at 222nm indicated More thermo stability of this protein at pH 6.8. The isoelectric point of this enzyme was determined as 5.85 using the chromatofocussing. In summary a lipoxygenase of HG purified to electrophoretic homogeneity has showed 95 +/- 5KDa molecular mass and had alpha-helix and beta pleated structures with a pH optimum of 6.80 and a pI value of 5.85. This enzyme showed preferred activity towards linolenic, acid.

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