转谷氨酰胺酶对鲤鱼肌原纤维蛋白功能特性的影响  

Influence of Transglutaminase on Functional Properties of Common Carp Myofibrillar Protein

作　　者：黄莉[1] 夏秀芳[1] 吕鸿鹄 费楠[1] 潘楠[1] 

机构地区：[1]东北农业大学食品学院,哈尔滨150030

出　　处：《食品工业》2014年第9期79-83,共5页The Food Industry

基　　金：黑龙江省博士后资助项目(LBH-Z11212);东北农业大学博士启动基金(2012RCB28)

摘　　要：将转谷氨酰胺酶添加到鲤鱼肌原纤维蛋白溶液中,在不同温度条件下热诱导凝胶,测定转谷氨酰胺酶-肌原纤维蛋白混合体系的凝胶特性(硬度、弹性、持水性、白度值)及肌原纤维蛋白浊度的变化,结果表明:当温度相同时,转谷氨酰胺酶-蛋白复合凝胶的硬度和弹性值随着转谷氨酰胺酶添加量的增大而升高,在60℃,70℃,80℃条件下,添加了不同添加量转谷氨酰胺酶的样品与对照组相比硬度和弹性都明显提高,差异显著(p<0.05),在80℃时分别提高了39.89%,31.72%。而随着转谷氨酰胺酶添加量的增加,凝胶持水性增大(p<0.05),最大值为90.43%,但转谷氨酰胺酶对凝胶的白度无明显的影响(p>0.05)。随着转谷氨酰胺酶添加量及温度的升高,肌原纤维蛋白的浊度增加,且效果显著。通过对SDS-PAGE凝胶电泳图谱结果表明,随着TG添加含量的增加,主要条带颜色变淡,说明TG加速了肌原纤维蛋白形成共价交联键,促进了蛋白凝胶三维立体网状的形成。因此,添加转谷氨酰胺酶可以有效提高肌原纤维蛋白的功能特性。The effects of transglutaminase on the gel properties of common carp myofibrillar protein Were studied. Gel properties （hardness, springiness, water-holding capacity, whiteness）, turbidity properties of myofibrillar protein was evaluated, respectively under different temperatures. Results indicated gel hardness and springiness of TG-protein composite increased gradually as the transglutaminase increased under the same temperature. Under the different temperature conditions （60 ℃, 70℃, 80℃）, hardness and springiness were improved compared with control group. Under the conditions of 80℃, hardness and springiness increased 39.89%, 31.72% compared with the control group, and effect was significantly （p〈0.05）. As the tmnsglutaminase increased, the water-holding capacity of gel increased （p〈0.05）, and the maximum was 90.43%, while effect on gel whiteness was no obviously （p〉0.05）. As the transglutaminase and temperature increased, the turbidity of common carp myofibrillar protein increased. The SDS-PAGE gel electrophoresis of MPI showed that TG catalyzed carp major protein, such as myosin heavy chain （MHC） forming covalent cross-linking bond. Therefore, transglutaminase can improved the gel properties of myofibrillar proteirL

关 键 词：转谷氨酰胺酶 肌原纤维蛋白 功能特性 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]