摘要
采用羟基自由基氧化体系（10μmol/L FeCl3、0.1mmol/L抗坏血酸、0.00～5.00mmol/L H2O2，24h孵育）对鸡胸肉肌原纤维蛋白进行不同程度的氧化，研究蛋白理化特性及热诱导凝胶特性的变化。结果表明：随着氧化剂浓度升高，羰基含量增加，巯基含量减少，说明蛋白氧化程度持续增大；H2O2浓度在0.00～0.10mmol/L之间升高，凝胶硬度显著增大（P＜0.05），蛋白溶解度和表面疏水指数呈下降趋势，但差异不显著（P＞0.05）；H2O2浓度在0.10～5.00mmol/L之间继续增大，蛋白溶解度下降，表面疏水指数升高，形成的热凝胶硬度和弹性均显著下降（P＜0.05）。上述结果表明氧化修饰会引起蛋白理化特性的改变，适度氧化可以改善肌原纤维蛋白的热凝胶特性。
Chicken breast myofibrillar protein was oxidized to different extents after 24 h of incubation in hydroxyl radicalgeneration systems （10 μmol/L FeCl3, 0.1 mmol/L ascorbic acid, and 0 to 5 mmol/L H2O2） and physico-chemical properties of the different oxidation products and properties of heat-induced gels prepared from them were comparatively investigated. The results showed that carbonyl content steadily increased and thiol group content declined with increasing H2O2 concentration, indicating continuous oxidation of the myofibrillar protein. Heat-induced gel hardness increased significantly as the concentration of H2O2 increased from 0.00 to 0.10 mmol/L while protein solubility and surface hydrophobicity declined. When H2O2 concentration increased up to 5 mmol/L, protein solubility as well as gel hardness and springiness significantly decreased （P 〈 0.05）, whereas the converse trend was observed for surface hydrophobicity. These results suggest that mild oxidation could improve the heat-induced gel formation of myofibrillar protein.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2013年第17期19-23,共5页
Food Science
基金
国家自然科学基金项目(31171707)
国家肉鸡产业技术体系建设项目(nycytx-42-G5)
关键词
氧化
肌原纤维蛋白
凝胶
理化特性
oxidation
myofibrillarprotein
gelation
physico-chemicalproperties
