Lipid oxidation in a chicken muscle model system: Oxidative response of lipid classes to iron ascorbate or methemoglobin catalysis

Citation
Rv. Sista et al., Lipid oxidation in a chicken muscle model system: Oxidative response of lipid classes to iron ascorbate or methemoglobin catalysis, J AGR FOOD, 48(5), 2000, pp. 1421-1426
Citations number
29
Categorie Soggetti
Agricultural Chemistry","Chemistry & Analysis
Journal title
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
ISSN journal
00218561 → ACNP
Volume
48
Issue
5
Year of publication
2000
Pages
1421 - 1426
Database
ISI
SICI code
0021-8561(200005)48:5<1421:LOIACM>2.0.ZU;2-X
Abstract
Catalysis by iron ascorbate and activated methemoglobin generated different oxidative responses in chicken muscle model systems. In iron ascorbate sys tems, large increases in hydroperoxides and thiobarbituric acid-reactive su bstances (TBARS) occurred during the initial stage of incubation. Thereafte r, iron ascorbate catalysis led to a slow increase in the oxidation of tria cylglcyerol (TG) and sarcoplasmic reticulum (SR) membrane lipids. By the en d of incubation, 24, 36, and 32% of the initial content of n-3 fatty acids in free fatty acids, TG, and SR single-lipid model systems catalyzed by iro n ascorbate had been lost. Reduced losses of n-3 fatty acids were observed in the SR and TG fractions (0 and 24%, respectively) when iron ascorbate mo del systems contained all three lipid fractions (mix). Hydroperoxides and T BARS in mode systems catalyzed by activated methemoglobin were characterize d by a lag phase during most of the incubation. Consistent with their role as antioxidants, losses of alpha-tocopherol (42-49%), gamma-tocopherol (36- 42%), and protein sulfhydryls (41-52%) were observed in model systems catal yzed by activated methemoglobin. SR and mix model systems were 30-50% slowe r to oxidize than TG model systems when activated methemoglobin served as t he catalytic agent.