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Lipid Oxidation in a Chicken Muscle Model System:  Oxidative Response of Lipid Classes to Iron Ascorbate or Methemoglobin Catalysis

Catalysis by iron ascorbate and activated methemoglobin generated different oxidative responses in chicken muscle model systems. In iron ascorbate systems, large increases in hydroperoxides and thiobarbituric acid-reactive substances (TBARS) occurred during the initial stage of incubation. Thereafte...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2000-05, Vol.48 (5), p.1421-1426
Main Authors: Sista, R. V, Erickson, M. C, Shewfelt, R. L
Format: Article
Language:English
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Summary:Catalysis by iron ascorbate and activated methemoglobin generated different oxidative responses in chicken muscle model systems. In iron ascorbate systems, large increases in hydroperoxides and thiobarbituric acid-reactive substances (TBARS) occurred during the initial stage of incubation. Thereafter, iron ascorbate catalysis led to a slow increase in the oxidation of triacylglcyerol (TG) and sarcoplasmic reticulum (SR) membrane lipids. By the end 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 iron 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 model systems contained all three lipid fractions (mix). Hydroperoxides and TBARS in model systems catalyzed by activated methemoglobin were characterized by a lag phase during most of the incubation. Consistent with their role as antioxidants, losses of α-tocopherol (42−49%), γ-tocopherol (36−42%), and protein sulfhydryls (41−52%) were observed in model systems catalyzed by activated methemoglobin. SR and mix model systems were 30−50% slower to oxidize than TG model systems when activated methemoglobin served as the catalytic agent. Keywords: Membrane; triacylglycerol; free fatty acid; sulfhydryl; tocopherol; hydroperoxide
ISSN:0021-8561
1520-5118
DOI:10.1021/jf9908897