冷藏过程中草鱼肌原纤维蛋白结构的变化  

Structural properties changes of myofibrillar protein from grass carp during cold storage

作　　者：李向红[1] 王发祥[1] 张付兰[1] 俞健[1] 王建辉[1] 刘永乐[1] 

机构地区：[1]长沙理工大学化学与生物工程学院,湖南省水生资源食品加工工程技术研究中心,湖南长沙410114

出　　处：《食品与发酵工业》2015年第10期177-181,共5页Food and Fermentation Industries

基　　金：国家自然科学基金资助项目(No.31201427,No.31301564);“十二五”国家科技支撑计划项目(No.2012BAD31B08);湖南省自然科学基金项目(No.12JJ6028)资助

摘　　要：采用扫描电镜(SEC)、傅里叶变换-红外光谱(FT-IR)、反相高效液相色谱(RP-HPLC)和Ellman's试剂比色法分析了草鱼肌原纤维蛋白显微结构、二级结构、表面疏水性及巯基和二硫键含量的变化。结果表明:冷藏前4 d,肌原纤维蛋白表面疏水性增加,二硫键含量减少,α-螺旋含量下降,β-折叠含量上升,显微结构逐渐扭曲但仍比较完整,说明其主要以变性为主;冷藏第6天开始,肌原纤维蛋白的β-折叠含量下降,无规则卷曲含量上升,分子颗粒逐渐断裂、穿孔或破碎,说明其变性更加严重,无序程度增加并逐渐降解。研究证明了草鱼肌原纤维蛋白冷藏过程中逐渐变性和降解的过程,为探讨冷藏过程中草鱼肌肉腐败形式提供了生物学证据。Changes in microstructure, secondary structure, surface hydrophobicity, sulfhydryl （SH） and disul- fide bond （S-S） content of myofibrillar protein during cold storage of grass carp were analyzed, using scanning elec- tron microscope （SEM）, fourier transform infrared spectroscopy （FT-IR）, reversed-phase high performance liquid chromatography （RP-HPLC） and Ellman~ colorimetric method, respectively. The results showed that the surface hy- drophobicity and content of/3-sheet increased, but the content of disulfide bond and a-helix decreased, and the micro- structure became distorted but still relatively complete at the first 4 days. This indicated that the main changes of myo- fibrillar protein were degeneration during this period. From the 6th day, the content of random coil increased but con- tent of/3-sheet decreased, and the protein particles was gradually fractured or broken, suggesting the degeneration and disorder degree of myofibrillar protein was increased, and degraded gradually. This is a new investigation on denatur- ation and degradation process of myofibrillar protein, and it provides some biological evidences to discuss corruption mechanism of grass carp during cold storage.

关 键 词：草鱼 肌原纤维蛋白 扫描电镜 红外光谱 表面疏水性 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]