Horseradish peroxidase degrades lipid hydroperoxides and suppresses lipid peroxidation of polyunsaturated fatty acids in the presence of phenolic antioxidants.
Linoleic acid hydroperoxide (LAOOH) was effectively degraded by horseradish peroxidase (HRP) in the presence of quercetin. Several natural phenolic antioxidants, such as quercetin, capsaicin, and alpha-tocopherol, acted as good hydrogen donors in the peroxidase reaction that occurs during lipid hydroperoxide degradation. However, glutathione, which is a non-phenolic antioxidant that acts as a hydrogen donor for glutathione peroxidase, could not suppress lipid peroxidation in the presence of HRP. Lipid hydroperoxides generated from eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) were also degraded with HRP in the presence of quercetin, and oxidative decomposition of DHA was suppressed by this reaction.
Department of Applied Biological Chemistry, Faculty of Agriculture, Kin-ki University, Nara, Japan. sirasaka@nara.kindai.ac.jp
Norifumi
N
Shirasaka
Hiromichi
H
Ohnishi
Keiko
K
Sato
Rie
R
Miyamoto
Takao
T
Terashita
Hajime
H
Yoshizumi
D000975:Antioxidants / Q000737:chemistry*; D004789:Enzyme Activation; D005231:Fatty Acids, Unsaturated / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D015227:Lipid Peroxidation; D008054:Lipid Peroxides / Q000737:chemistry*; D010636:Phenols / Q000737:chemistry*; D013379:Substrate Specificity
D000975:Antioxidants; D005231:Fatty Acids, Unsaturated; D008054:Lipid Peroxides; D010636:Phenols; D006735:Horseradish Peroxidase