College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China.
College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China.
Meat Sci. 2014 Apr;96(4):1432-9. doi: 10.1016/j.meatsci.2013.12.001. Epub 2013 Dec 12.
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 (AAPH1mM) enhanced the water-holding capacity (WHC) and texture properties of gels, while further oxidation (AAPH>3mM) significantly reduced the gel quality.
AAPH 衍生的（2,2'-偶氮双（2-脒基丙烷）二盐酸盐）过氧自由基被选为脂质过氧化的代表性自由基，以研究氧化修饰对分离的猪肌原纤维蛋白结构以及其流变和胶凝特性的影响。肌原纤维蛋白与浓度逐渐增加的 AAPH 孵育导致羰基含量和 SH→S-S 转换逐渐增加（p<0.05）。SDS-PAGE 的结果表明，中等（1mM）和相对较高（>3mM）浓度的 AAPH 分别诱导肌球蛋白聚集和肌球蛋白、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化的粘弹性模式没有显著影响（p>0.05）。适度的氧化修饰（AAPH1mM）增强了凝胶的持水能力（WHC）和质地特性，而进一步的氧化（AAPH>3mM）则显著降低了凝胶质量。
