高压均质条件下大豆蛋白热聚集体结构和乳化特性研究  

Effects of High-pressure Homogenization on Structural and Emulsifying Properties of Soybean Protein Thermal Aggregates

作　　者：郭增旺 郭亚男 李柏良 江连洲[1] 王中江[1] 刘军 GUO Zengwang;GUO Ya’nan;LI Bailiang;JIANG Lianzhou;WANG Zhongjiang;LIU Jun(College of Food Science,Northeast Agricultural University,Harbin 150030,China;Linyi Yuwang Plant Protein Co.,Ltd.,Dezhou 253000,China;Kedong Yuwang Soybean Protein Food Co.,Ltd.,Qiqihar 161000,China)

机构地区：[1]东北农业大学食品学院,哈尔滨150030 [2]临邑禹王植物蛋白有限公司,德州253000 [3]克东禹王大豆蛋白食品有限公司,齐齐哈尔161000

出　　处：《农业机械学报》2021年第4期351-358,374,共9页Transactions of the Chinese Society for Agricultural Machinery

基　　金：山东省重点研发计划项目(2018YYSP026);中国科协第五届(2019—2021年度)青年人才托举工程项目(2019QNRC001);哈尔滨市雏鹰计划项目(CY2019JH020004);黑龙江省普通本科高等学校青年创新人才培养计划项目(UNPYSCT-2018163);黑龙江省博士后科研启动资金项目(LBH-Q2008);山东省德州市大禹英才项目。

摘　　要：以大豆蛋白为原料,采用加热处理(100℃、20 min)制备可溶性热聚集体,分别对其进行高压均质(0、30、60、90、120 MPa)处理,探究高压均质技术(HPH)对大豆蛋白热聚集体结构特性(粒径分布、浊度、骨架结构、二三级结构、疏水性、电位、巯基)、流变学表征和乳化特性(乳化活性和乳化稳定性)的影响。结果表明:低压力的高压均质处理可以促进热聚体发生再聚集,使粒径和浊度逐渐增大、骨架结构变密、无序结构增多,并且发生再聚集,其疏水性降低,ζ-电位绝对值和二硫键含量升高,进而导致乳化活性提高;而高压力的高压均质处理会导致热聚集体的二硫键和骨架结构发生大量断裂,分子结构展开,疏水性位点大量暴露,导致疏水性增强、蛋白分子链变短、粒径和ζ-电位绝对值降低,进而导致乳化活性降低。本研究可为大豆蛋白功能性质的改性及高压均质在热聚集体行为调控方面的应用提供参考。To investigate the effect of high-pressure homogenization on the structure and emulsification of soybean protein,high-pressure homogenization( HPH) treatment at 20 min and 100℃ were applied to the soybean protein thermal aggregates( HSPIs). The changes of HSPIs structure characteristics( particle size distribution, turbidity, skeleton structure, secondary and tertiary structure, hydrophobicity,potential,sulfhydryl) and emulsification characteristics( rheological characterization,emulsification and emulsification temperature) were assayed. The results showed that compared with the heat soluble aggregates degree,the lower pressure of HPH can promote the re-aggregation of the thermal induced HSPIs,which resulted in the increase of particle size and turbidity,the densification of HSPIs skeleton structure. Along with the re-aggregation,the HSPIs disordered structure,particle ζ-potential and protein peptide chains disulfide bond content were increased,and resulted in the increase of emulsifying activity and decrease of hydrophobicity. While on HPH,strong strength homogenization can lead the disulfide bond and skeleton structure of HSPIs broken, the protein spatial structure was opened, and the hydrophobic sites were exposed,which resulted in enhancement of hydrophobicity,shortening of protein peptide chain,decrease of particle size and the increase of ζ-potential,and then the decrease of emulsifying activity of HSPIs. The results for the modification of soybean protein functional properties and the application by high-pressure homogenization changed HSPIs.

关 键 词：大豆蛋白 热聚集体 高压均质 结构特性 乳化特性 

分 类 号：TS201.1[轻工技术与工程—食品科学]