Species-Specific Myoglobin Oxidation

被引：29

作者：

Yin, Shuang ^{[1
]}

Faustman, Cameron ^{[1
]}

Tatiyaborworntham, Nantawat ^{[1
]}

Ramanathan, Ranjith ^{[1
]}

Maheswarappa, Naveena B. ^{[2
]}

Mancini, Richard A. ^{[1
]}

Joseph, Poulson ^{[3
]}

Suman, Surendranath P. ^{[3
]}

Sun, Qun ^{[4
]}

机构：

[1] Univ Connecticut, Dept Anim Sci, Storrs, CT 06269 USA

[2] Natl Res Ctr Meat, Hyderabad 500039, Andhra Pradesh, India

[3] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40536 USA

[4] Sichuan Univ, Coll Life Sci, Chengdu 610041, Peoples R China

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2011年 / 59卷 / 22期

关键词：

myoglobin; lipid oxidation; 4-hydroxy-2-nonenal; mass spectrometry; meat color; LIPID OXIDATION; REDOX INSTABILITY; OXYMYOGLOBIN; PORCINE; BOVINE; ALDEHYDES; FORMS;

D O I：

10.1021/jf202844t

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

The effect of the lipid oxidation product, 4-hydroxy-2-nonenal (HNE), on oxidation of oxymyoglobin (OxyMb) from seven different meat-producing species was investigated. Relative to controls, HNE increased OxyMb oxidation within all species (p < 0.05) at both 25 and 4 degrees C, pH 5.6. The relative effect of HNE was greater for myoglobins (Mbs) that contained 12 1 histidine (His) residues than for those that contained 9 His residues (p < 0.05); HNE efficacy in all species except chicken and turkey decreased with time. Mono-HNE adducts were detected in all species except chicken and turkey. In general, HNE alkylation increased the Mbs' ability to accelerate lipid oxidation in a microsome model. However, neither an HNE nor a Mb species dependent effect was observed. Results suggested that microsome model system associated lipid oxidation overshadowed HNE and species effects on OxyMb oxidation observed in lipid-free systems.

引用

页码：12198 / 12203

页数：6

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