蛋清蛋白热诱导凝胶特性研究  

Study on Heat-Induced Gel Characteristics of Egg White Protein

作　　者：杨雅婧 徐琳 杨须跃 杨须强 王超 陈振家[1] YANG Ya-jing;XU Lin;YANG Xu-yue;YANG Xu-qiang;WANG Chao;CHEN Zhen-jia(College of Food Science and Engineering,Shanxi Agricultural University,Jinzhong 030801,China;Jiangsu Xiangdao Food Co.,Ltd.,Xuzhou 221600,China)

机构地区：[1]山西农业大学食品科学与工程学院,山西晋中030801 [2]江苏香道食品有限公司,江苏徐州221600

出　　处：《中国调味品》2023年第11期5-10,共6页China Condiment

基　　金：2019年江苏省“双创计划”(224345)。

摘　　要：以鸡蛋为研究对象,将蛋清于80,90,100℃下分别加热10,20,30 min制备凝胶,通过质构仪、SDS-PAGE、红外光谱、扫描电子显微镜等仪器,对其组织结构、持水力、蛋白质亚基组成、凝胶作用力组成、总巯基含量、二级结构和微观结构进行测定,分析蛋清蛋白的凝胶特性。结果表明,随着加热温度的上升和时间的延长,硬度、胶黏性和咀嚼性呈现先上升后下降的趋势,在90℃下加热20 min时均达到了最大值,硬度为12.18 N,胶黏性为5.72 N,咀嚼性为54.96 mJ;持水力逐渐降低,在100℃下加热20 min时最低,为68.7%;可溶性蛋白含量先降低后升高,可溶性蛋白亚基条带增加;蛋清蛋白凝胶作用力中主要是疏水作用和二硫键,占比达80%以上,随着温度的升高,疏水作用比例呈上升趋势;凝胶的总巯基含量呈下降趋势,最低达到12.69μmol/L;在90℃下加热20 min时,β-折叠含量由32.16%增加到56.31%,β-转角含量由40.03%减少到18.24%,蛋白质的二级构象发生了显著的变化。With egg as the research subject,egg white is heated at 80,90,100℃for 10,20,30 min respectively to prepare gel.The tissue structure,water holding capacity,protein subunit composition,gel force composition,total sulfhydryl content,secondary structure and microstructure of the gel are determined by texture analyzer,SDS-PAGE,infrared spectra and scanning electron microscope,and the gel characteristics of egg white protein are analyzed.The results show that with the increase of heating temperature and the extension of time,the hardness,adhesiveness and chewiness increase firstly and then decrease,they all reach the maximum values when being heated at 90℃for 20 min,with the hardness of 12.18 N,adhesiveness of 5.72 N and chewiness of 54.96 mJ.The water holding capacity decreases gradually,reaching a minimum value of 68.7%when being heated at 100℃for 20 min.The content of soluble protein decreases firstly and then increases,and the bands of soluble protein subunits increase.Hydrophobic action and disulfide bond are the main gel forces in egg white protein,accounting for more than 80%.With the increase of temperature,the proportion of hydrophobic action increases.The total sulfhydryl content of the gel shows a downward trend,reaching the minimum value of 12.69μmol/L.When being heated at 90℃for 20 min,the content ofβ-sheet increases from 32.16%to 56.31%,and the content ofβ-turn decreases from 40.03%to 18.24%.The secondary conformation of protein changes significantly.

关 键 词：鸡蛋 凝胶作用力 二级结构 扫描电镜 

分 类 号：TS201.21[轻工技术与工程—食品科学]