摘要
通过亚基组成、热力学性质、表面疏水性和Ca2+-ATPase活性的变化分析,评价了草鱼(Ctenopharyngodon idellus)肌原纤维蛋白在冷藏过程中的变化。结果表明:冷藏前期草鱼肌原纤维表面疏水性增加,说明蛋白逐渐变性导致更多的疏水性基团暴露出来,而第6 d后又大幅降低,可能与其部分降解为小分子并聚合有关;而Ca2+-ATPase活性在冷藏前6 d显著下降,进一步说明冷藏前期肌原纤维蛋白变性程度增加;SDS-PAGE分析表明草鱼肌原纤维蛋白的亚基组成变化不大,但其蛋白含量在冷藏过程中呈先增加后下降的趋势,同时部分蛋白条带信号时有时无,也说明冷藏过程中既存在大分子亚基一定程度的降解,也存在小分子亚基聚合的情况;冷藏过程中草鱼肌原纤维蛋白的热力学性质没有明显的变化,表明冷藏对其热稳定性影响不大。
Through analyzing the variation of protein subunit composition,thermodynamic properties,surface hydrophobicity and Ca2 ＋-ATPase activity of myosin,the changes in myofibrillar proteins of grass carp during chilling storage were investigated. The results showed that with the extension of chilling storage time,the surface hydrophobicity of myofibrillar proteins was increased at first and then descended sharply and the Ca2 ＋- ATPase activity of myosin was declined significantly, indicating that the degree of myofibrillar protein denaturation was augmented gradually. SDS-PAGE analysis revealed that there was little change in subunits composition of myofibrillar protein,but its total content increased at first but later decreased,and at the same time,part of the protein band signal was occasionally detected,suggesting some degree of degradation with macromolecular subunits and polymerization with small molecular subunit might coexist during cold storage period. Besides,there was no apparent change in thermodynamic properties of the myofibrillar protein of different storage time,indicating that cold storage had little effect on its thermal stability.
出处
《食品工业科技》
CAS
CSCD
北大核心
2015年第18期82-86,共5页
Science and Technology of Food Industry
基金
国家自然科学基金项目(31201427
31301564)
国家科技支撑计划项目(2012BAD31B08)
湖南省自然科学基金项目(12JJ6028)
关键词
草鱼
肌原纤维蛋白
表面疏水性
差示扫描量热法
冷藏
grass carp
myofibrillar proteins
hydrophobicity
differential scanning calorimetry
chilling storage
