肌原纤维
化学
肌球蛋白
氧化磷酸化
原肌球蛋白
激进的
变性(裂变材料)
色谱法
肌节
脂质过氧化
氧化应激
生物化学
核化学
心肌细胞
生物
内分泌学
作者
Feibai Zhou,Ming Zhao,Haifeng Zhao,Weizheng Sun,Chun Cui
出处
期刊:Meat Science
[Elsevier]
日期:2014-04-01
卷期号:96 (4): 1432-1439
被引量:126
标识
DOI:10.1016/j.meatsci.2013.12.001
摘要
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.
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