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Calcium activation of peanut lipoxygenase

  • Published:
Lipids

Abstract

Peanut lipoxygenase isozyme 1 (pH optimum, 8.3) was strongly activated by 0.5–1.0 mM Ca++, and the rate of activation was maximum when the ratio of substrate to Ca++ was ca. 2∶1. Peanut lipoxygenase isozymes 2 and 3 (pH optima, 6.2) were activated by calcium but did not have an optimum level of activity. Calcium differentially activated peanut lipoxygenase causing the rate of pentane production to increase much more rapidly than the rate of oxygen consumed by the enzyme reaction. At pH 6.2, in the absence of calcium, the percentages of the hydroperoxide isomers produced by peanut lipoxygenase were 74.9% 13-hydroperoxycis-9,trans-11-octadecadienoic acid (13 LOOHcis-trans), 2.6% 13-hydroperoxytrans-9,trans-11-octadecadienoic acid (13 LOOHtrans-trans) and 22.5% 9-hydroperoxy 10, 12-octadecadienoic acid (9 LOOH). The presence of 1 mM Ca++ at pH 6.2 did not significantly affect the percentage distribution of the hydroperoxides produced. However, at pH 8.3, the percentage distribution of hydroperoxides produced was 45.2% 13 LOOHcis-trans, 10.9% 13 LOOHtrans-trans and 43.9% 9 LOOH in the absence of Ca++ and 57.0% 13 LOOHcis-trans, 8.0% 13 LOOHtrans-trans and 35.0% 9 LOOH in the presence of 1 mM Ca++.

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Author information

Authors and Affiliations

  1. Departments of Biological and Agricultural Engineering and Botany, North Carolina State University and Southern Region, ARS, USDA, 27607, Raleigh, NC

    M. S. Nelson, H. E. Pattee & J. A. Singleton

Authors
  1. M. S. Nelson
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  2. H. E. Pattee
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  3. J. A. Singleton
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Additional information

Paper No. 5110 of the Journal of the North Carolina Agricultural Experiment Station, Raleight, NC 27607.

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Nelson, M.S., Pattee, H.E. & Singleton, J.A. Calcium activation of peanut lipoxygenase. Lipids 12, 418–422 (1977). https://doi.org/10.1007/BF02533626

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  • DOI: https://doi.org/10.1007/BF02533626

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