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​Cowpea lipoxygenase: Part 1 Physiochemical Characterization

The Bulletin of Philippine Biochemical Society
​Volume 2, Issue 1, 1979, Pages 1-12
​
Authors
Truong Van Den*, Leoncio C. Raymundo* and Evelyn Mae Tecson-Mendoza**
        
*Dept. of Food Science and Technology
**Institute of Plant Breeding, College of Agriculture, University of the Philippines - Los Baños, College, Laguna
 
Abstract
              Lipoxygenase (linoleate: oxygen oxidoreductase E.C.1.13.11.12) level was determined in ten varieties of cowpea, five varieties of soybean, and six varieties of winged bean. Cowpea lipoxygenase specific activity was highest (205 – 316 units/mg protein) as compared to that of winged bean (14 – 30 units/mg protein) and soybean (11- 48 units/mg protein).
          Crude cowpea lipoxygenase was observed to have optimum activity at about pH 6.2 and 30°C. The apparent Km and substrate concentration at Vmax of this enzyme which follows Michaelis-Menten kinetics were 0.195 x 10-3 and 1.6 x 10-3 M, respectively.
             Lipoxygenase activity was located in 40 – 50% and 50 – 60% ammonium sulfate precipitates with 3 and 5 fold enrichment in said fractions.
       Disc gel electrophoresis followed by specific enzyme staining revealed four isozymes of cowpea lipoxygenase with a major isozyme Rf = 0.21 – 0.27. The average molecular weight of this enzyme is 68,000 daltons as shown by Sephadex G – 50 gel chromatography.
         The possible role of lipoxygenase in the formation of the strong beany flavor of cowpea is discussed.
​ (1979)
 
To cite this article
V.A Truong, L.C. Raymundo and E.M. Tecson-Mendoza​, Cowpea lipoxygenase: Part 1 Physiochemical Characterization, The Bulletin of Philippine Biochemical Society, Vol. 2, No. 1, 1979, pp. 1-12.      
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