Biochemistry of lipoxygenase in relation to food quality.
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.
D000693:Anaerobiosis; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D005433:Flour; D005502:Food / Q000592:standards; D005638:Fruit; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008055:Lipids; D008084:Lipoxygenase / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000201:enzymology; D013025:Glycine max; D013379:Substrate Specificity; D014675:Vegetables; D014835:Volatilization
D007527:Isoenzymes; D008055:Lipids; D008084:Lipoxygenase