Enzymatic oxidations of linoleic acid and glycerol‐1‐monolinoleate in doughs and flour‐water suspensions
1970; Wiley; Volume: 47; Issue: 9 Linguagem: Inglês
10.1007/bf02639001
ISSN1558-9331
Autores Tópico(s)Biochemical and biochemical processes
ResumoAbstract Enzymatic oxidations of linoleic acid and glycerol‐1‐monolinoleate, and the products formed by these oxidations in flour‐water suspensions and doughs were studied. Oxidation of linoleic acid leads through simultaneous reactions to two isomeric hydroperoxy‐octadecadienoic acids and two isomeric hydroxy‐epoxy‐octadecenoic acids. Reduction of the former leads to hydroxyoctadecadienoic acid, while hydrolysis of the latter yields trihydroxy‐octadecenoic acids. The hydroperoxy acids are formed by the enzyme lipoxygenase (E.C. 1.13.1.13), whereas the hydroxy‐epoxy acids are formed by combined action of lipoxygenase and an unknown factor Y. This factor Y is localized in the gluten fraction. Oxidation of glycerol‐1‐monolinoleate gives a product having a hydroperoxy group and a cis,trans conjugated diene bond. The oxidation of glycerol‐1‐monolinoleate is probably a lipoxygenase reaction.
Referência(s)