摘要
利用罗非鱼鱼皮制备4种分子质量的明胶蛋白,测定添加明胶蛋白对鲢鱼鱼糜凝胶性质的影响。结果表明含有α肽链的明胶蛋白,可以提高鱼糜制品的凝胶强度、质构和保水性能,并且对鱼糜制品的色泽无明显的影响。将α肽链被完全降解的明胶蛋白添加到鱼糜中,制备的鱼糜制品物理性质没有发生显著的变化,但色泽稍微变黄。根据蛋白变性剂中溶解的鱼糜凝胶蛋白的SDS-PAGE图谱以及利用石蜡包埋组织切片法获得的鱼糜凝胶微观组织结构的变化,发现高分子明胶蛋白不会干扰鱼糜中肌球蛋白重链(MHC)和肌动蛋白之间的交联,而小分子明胶蛋白容易填充到鱼糜凝胶的网络结构中,阻碍MHC和肌动蛋白之间的相互作用。傅里叶变换红外光谱(FTIR)分析表明鱼糜蛋白与明胶蛋白之间主要通过氢键结合。
Gelatins with different molecular weight distribution were prepared from tilapia skin, and the effect of these gelatins on gel properties of silver carp surimi was investigated. The gel strength, texture and water holding capaci- ty of silver carp surimi gels were improved by adding skin gelatins containing α-subunit, while the color was not changed remarkably. On the other hand, when α-subunit of skin gelatins was degraded completely, no obvious change in the physical properties of surimi gels was observed irrespective of skin gelatins incorporation. Furthermore, the silver carp surimi gels incorporated with low molecular weight skin gelatin tended to have slight yellow color. Based on the re- suits of SDS-PAGE pattern of the soluble fractions in protein denaturant solution and the microstructure of surimi gels using paraffin embedding, it was revealed that the cross-linking between myosin heavy chain （MHC） and actin in silver carp surimi gels was not influenced by adding high molecular weight skin gelatin, while low molecular weight skin gelatin can fill pores in the gel network formed from surimi proteins, leading to hinder the interaction between MHC and actin. The interactions between surimi protein and skin gelatin were mainly through hydrogen bonds based on the data of Fourier transform infrared（FTIR） spectra.
出处
《中国食品学报》
EI
CAS
CSCD
北大核心
2013年第8期83-90,共8页
Journal of Chinese Institute Of Food Science and Technology
基金
福建省高校新世纪优秀人才支持计划(JA11143)
厦门市科技计划项目(3502Z20123025)
集美区科技项目(20117A04)
关键词
鲢鱼鱼糜
凝胶性质
鱼皮明胶
作用机理
Silver carp surimi
gel-forming properties
fish skin gelatin
forming mechanism
