Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals.
Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals.
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DOI：
10.1016/j.meatsci.2013.12.001
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发表时间：
2014-04
期刊：
影响因子：
7.1
通讯作者：
Feibai Zhou;Mouming Zhao;Haifeng Zhao;Weizheng Sun;Chun Cui
中科院分区：
文献类型：
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作者：
Feibai Zhou;Mouming Zhao;Haifeng Zhao;Weizheng Sun;Chun Cui
选择AAPH衍生的（2,2'-偶氮双（2-脒基丙烷）二盐酸盐）过氧化自由基作为脂质过氧化的代表性自由基，研究氧化修饰对分离的猪肌原纤维蛋白结构及其流变学和胶凝特性的影响。随着 AAPH 浓度的增加，肌原纤维蛋白的孵育导致羰基含量和 SH → S-S 转化逐渐增加 (p< 0.05)。 SDS-PAGE 结果表明，中等浓度 (~ 1 mM) 和相对高浓度 (> 3 mM) 的 AAPH 分别诱导肌球蛋白聚集以及肌球蛋白、肌钙蛋白和原肌球蛋白变性。这些结构变化导致肌原纤维蛋白凝胶化的变化。低水平的蛋白质氧化（AAPH≤0.5mM）对肌原纤维蛋白凝胶的粘弹性模式没有显着影响（p>0.05）。中等氧化修饰（AAPH ~ 1 mM）增强了凝胶的持水能力（WHC）和质地特性，而进一步氧化（AAPH > 3 mM）则显着降低了凝胶质量。
AAPH-derived (2,2′-azobis (2-amidinopropane) dihydrochloride) peroxyl radicals were selected as representative free radicals of lipid peroxidation to investigate the effects of oxidative modifications on isolated porcine myofibrillar protein structures as well as their rheological and gelling properties. Incubation of myofibrillar protein with increasing concentrations of AAPH resulted in a gradual increase (p< 0.05) in carbonyl content and SH → S–S conversion. Results from SDS-PAGE indicated that medium (~ 1 mM) and relatively high (> 3 mM) concentrations of AAPH induced aggregation of myosin and denaturation of myosin, troponin and tropomyosin, respectively. These structural changes resulted in changes on gelation of myofibrillar protein. Low level protein oxidation (AAPH ≤ 0.5 mM) had no remarkable effect (p> 0.05) on the viscoelastic pattern of myofibrillar protein gelation. Moderate oxidative modification (AAPH ~ 1 mM) enhanced the water-holding capacity (WHC) and texture properties of gels, while further oxidation (AAPH > 3 mM) significantly reduced the gel quality.