A renewed interest in lipoxygenase has led to detailed studies of its isoenzymes, substrate specificity, and the nature of its reaction products. Lipoxygenase is highly specific for cis,cis-1,4-pentadiene systems such as linoleic, linolenic, and arachidonic acid (or ester) and catalyzes the formation of the corresponding hydroperoxides with a cis,-trans-conjugated diene system. The hydroperoxides can then undergo enzymic or spontaneous degradation, producing a range of carbonyl compounds. This review will discuss the biochemical properties of this enzyme and its contribution to the quality of raw and processed food products. An attempt has been made to discuss both the desirable and undesirable effects associated with the action of lipoxygenase, citing specific food examples where appropriate.
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Department of Biochemistry, Institute of Chemistry, University of São Paulo, Av. Prof. Lineu Prestes 748, 05508-000 São Paulo, Brazil.
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Medical College of Hebei University of Engineering, Handan, China.
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Lomonosov Institute of Fine Chemical Technologies, MIREA-Russian Technological University, Vernadskogo pr. 86, Moscow 119571, Russia.
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Eye Research Institute, Oakland University, Rochester, MI 48309, USA.
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