Inhibition of linoleic acid oxidation by interaction with a protein-rich oat fraction.
A protein-rich fraction from oat was found to protect linoleic acid against oxidation in an aqueous suspension containing soybean lipoxygenase-1 and micellar linoleic acid. In this system the oat fraction reduced the initial oxidation rate of linoleic acid by 50% when the oat fraction/linoleic acid ratio was 5:1 (w/w). The oat fraction did not act on the lipoxygenase enzyme but reduced the concentration of linoleic acid that serves as a substrate for lipoxygenase-1. To achieve the reduction in the oxidation rate a contact between linoleic acid and the oat fraction was required. The efficiency of the protection was dependent on the duration of this contact: the maximum protection was reached after a 5-min incubation period. However, total cessation of oxidation was not reached with any concentration of the oat fraction, indicating that the oxidizible and non-oxidizible forms of linoleic acid are in equilibrium. Because lipoxygenase-1 prefers the monomeric form of the substrate, the present findings agree with the hypothesis that the oat fraction reduces the concentration of monomolecular form of substrate. In most food systems monomolecular free linoleic acid is liberated slowly and at relatively low concentrations, therefore, even a small amount of the oat fraction would guard the system from oxidative deterioration.
Lehtinen
P
P
Helsinki University of Technology, Laboratory of Biochemistry and Microbiology, Post Office Box 6100, FIN-02015 TKK, Finland. Pekka.Lehtinen@hut.fi
Laakso
S
S
D018554:Avena; D005227:Fatty Acids / Q000737:chemistry; D007700:Kinetics; D019787:Linoleic Acid / Q000737:chemistry*; D008084:Lipoxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry*
D005227:Fatty Acids; D010940:Plant Proteins; D019787:Linoleic Acid; D008084:Lipoxygenase