热诱导大豆分离蛋白对肌原纤维蛋白凝胶特性的影响  

Effects of heat-induced soy protein isolate on gel properties of myofibrillar proteins

作　　者：武雅琴 王莉莎 邹咪 包海蓉[1,2,3] WU Yaqin;WANG Lisha;ZOU Mi;BAO Hairong(College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China;ShanghaiEnigeering Research Center of Aguatic-Product Processing&Preservation,Shanghai 201306,China;Laboratory of Quality and Satefy Risk Assessment for Aguatic Products on Storage and Preservation(Shanghai),Ministry of Agricuture,Shanghai 201306,China)

机构地区：[1]上海海洋大学食品学院,上海201306 [2]上海水产品加工及贮藏工程技术研究中心,上海201306 [3]农业部水产品加工贮藏保鲜质量安全风险评估实验室(上海),上海201306

出　　处：《食品与发酵工业》2019年第10期60-65,共6页Food and Fermentation Industries

基　　金：国家高技术研究发展计划“863”计划(2012AA092302);中央级公益性科研院所业务费专项资金(东海水产研究所)资助项目(2018M04)

摘　　要：大豆分离蛋白(soybean protein isolate,SPI)经60、80和95 ℃热处理,分别与鱼肌原纤维蛋白(myofibrillar protein,MP)按质量比1∶ 3(总蛋白质量浓度45 g/L)热诱导得到混合蛋白凝胶。结果表明,从流变特性来看,与天然大豆分离蛋白复合凝胶(MP-N-SPI)相比,MP-SPI(80 ℃)的储能模量值( G ′)( P <0.05)显著上升,而MP-SPI(60 ℃和95 ℃)却低于MP-N-SPI。在MP中加入SPI后,复合凝胶的持水性均高于单纯MP,适宜的热诱导温度SPI(80 ℃),可以明显改善复合凝胶的持水力(water holding capacity,WHC)( P <0.05)。从质构特性看出, MP-SPI (95 ℃)的硬度显著提升。电泳图谱显示,MP-N-SPI凝胶条带与单纯MP无明显差异,MP-SPI(80 ℃和 95 ℃)条带比MP-N-SPI和MP-SPI(60 ℃)浅,说明预热SPI(80 ℃或95 ℃)容易与MP相互作用。化学力测定显示,预热大豆蛋白与MP的凝胶网络形成主要是疏水作用的结果,而氢键和二硫键不是复合凝胶形成的主要化学力。由此可见,适宜的热诱导大豆分离蛋白,可以明显改善复合凝胶的特性。Soybean protein isolate (SPI) was treated at 60, 80, and 95 ℃, respectively, with fish myofibrillar protein (MP) in a ratio of 1∶ 3 (total protein concentration 45 g/L), to form a mixed protein gel by heat induction. The results showed that compared with natural soy protein isolate gel (MP-N-SPI), the storage modulus value ( G′) of MP-SPI at 80 ℃ increased significantly ( P <0.05), while the value was lower at 60 and 95 ℃. After adding SPI to MP, the water holding capacity (WHC) of the composite gel was higher than that of MP alone. A suitable heat-induced temperature of SPI (80 ℃) could significantly improve the WHC of the composite gel ( P <0.05). Moreover, the hardness of MP-SPI at 95 ℃ significantly improved. The SDS-PAGE showed that there were no significant differences in bands between MP-N-SPI and MP alone. The bands of MP-SPI at 80 and 95 ℃ were lighter than MP-N-SPI and MP-SPI at 60 ℃, which indicated that pre-heated SPI at 80 or 95 ℃ was easy to interact with MP. Chemical force measurements showed that the gel network of preheated soy protein and MP mainly formed by hydrophobic interaction. In conclusion, a suitable heat-induced SPI can significantly improve the properties of the composite gel.

关 键 词：大豆分离蛋白 鱼肌原纤维蛋白 凝胶特性 化学力 

分 类 号：TS201.21[轻工技术与工程—食品科学]