摘要
采用拉曼光谱技术测定凡纳滨对虾肌动球蛋白冻藏过程中的构象变化,解析蛋白质构象特征振动。测定结果表明,南美白对虾肌肉蛋白二级结构主链构象由酰胺I带（1 600~1 700 cm-1）和936 cm-1表征。在-40℃冻藏4周,I936由新鲜时的0.4682降到0.2336;在-18℃冻藏4周,I936降到0.2278;在-10℃I936降为0.2136,分别下降了50.13%,51.35%,54.38%。表征肌动球蛋白中酪氨酸残基的谱带出现在641 826 cm-1和854 cm-1,新鲜肌动球蛋白I854/I826的比值为1.098,冻藏过程中比值总体呈增加趋势。脂肪族氨基酸的C-H伸缩与弯曲分别在2800~3 100 cm-1与1 440~1 465 cm-1区间。-40℃冻藏4周,C-H键2 935 cm-1处的相对强度由新鲜时的3.7545,降到2.5065;-18℃冻藏4周降到1.8299;-10℃降为1.4436,分别下降了33.24%,51.26%,61.55%。拉曼光谱特征谱带的减弱甚至消失,可表观冻藏过程虾肉蛋白结构变化趋势与变化程度。
The actomyosin structure change in white shrimp（Litopenaeus vannamei） during the process of frozen storage was determined using Raman spectroscopy. The main chain conformation of white shrimp muscle protein secondary structure was characterized by amide I band（1 600-1 700 cm-1） and 936 cm-1. The relative intensity of the 936 cm-1band dropped from 0.4682 in the fresh shrimp to 0.2336, 0.2278 and 0.2136 in the frozen shrimp stored for 4 weeks at-40℃,-18 ℃ and-10 ℃, which fell by 50.13%, 51.35%, and 54.38%, respectively. Characteristic peak of tyrosine residues of the actomyosin appeared in 641 cm-1, 826 cm-1and 854 cm-1. This relative intensity ratio, determined by the Raman signals around 854 and 826 cm-1, I854/ I826, increased gradually during frozen storage. The C-H stretching and bending of aliphatic amino acids are in 2 800-3 100 cm-1and 1 440-1 465 cm-1interval respectively. Frozen under-40℃ for 4 weeks, C-H bond at 2 935 cm-1relative intensity decreased from 3.7545 to 2.5065, while that of the samples frozen under-18 ℃ and-10 ℃ decreased to 1.8299 and 1.4436, respectively. The Raman spectral bands weakened or even disappeared of during frozen storage indicating the change of shrimp actomyosin structure.
出处
《中国食品学报》
EI
CAS
CSCD
北大核心
2016年第2期218-223,共6页
Journal of Chinese Institute Of Food Science and Technology
基金
国家自然科学基金项目(31000798)
广东省海洋渔业科技推广专项(A200901I03)
关键词
凡纳滨对虾
拉曼光谱
肌动球蛋白
构象
冻藏
Litopenaeus vannamei
Raman spectroscopy
actomyosin
structure
frozen storage
