Effect of Heating Oxymyoglobin and Metmyoglobin on the Oxidation of Muscle Microsomes

被引:35
作者
Bou, Ricard [1 ,2 ]
Guardiola, Francesc [2 ]
Codony, Rafael [2 ]
Faustman, Cameron [3 ]
Elias, Ryan J. [1 ]
Decker, Eric A. [1 ]
机构
[1] Univ Massachusetts, Dept Food Sci, Amherst, MA 01003 USA
[2] Univ Barcelona, Dept Food Sci & Nutr, Fac Pharm, XaRTA,INSA, E-08028 Barcelona, Spain
[3] Univ Connecticut, Dept Anim Sci, Storrs, CT 06269 USA
关键词
Oxymyoglobin; metmyoglobin; lipid oxidation; meat; antioxidant; iron;
D O I
10.1021/jf8009848
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Myoglobin (Mb) and its iron have been proposed to be major prooxidants in cooked meats. To understand the mechanisms and differentiate between the prooxidant and antioxidant potential of oxymyoglobin (OxyMb) and metmyoglobin (MetMb), their prooxidant activity, iron content, solubility, free radical scavenging activity, and iron binding capacity were determined as a function of thermal processing. The ability of native and heat denatured OxyMb and MetMb to promote the oxidation of muscle microsomes was different. MetMb promoted lipid oxidation in both its native and denatured states. Conversely, OxyMb became antioxidative when the protein was heated to temperatures 75 degrees C. The increased antioxidant activity of heat denatured OxyMb was likely due to a decrease in its prooxidative activity due to its loss of solubility. These data show that the impact on oxidative reactions of Mb is the result of the balance between its antioxidant and prooxidant activities.
引用
收藏
页码:9612 / 9620
页数:9
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