不同热处理温度下大豆11S球蛋白Zeta电位、粒径和红外光谱分析  

Analysis of Zeta Potential, Particle Size and Infrared Spectroscopy of 11S Glycinin at Different Heat Treatment Temperatures

作　　者：齐宝坤[1] 赵城彬[2] 江连洲[1] 徐靓[1] 李红[1] 李杨[1] QI Baokun;ZHAO Chengbin;JIANG Lianzhou;XU Liang;LI Hong;LI Yang(College of Food Science,Northeast Agricultural University,Harbin 150030,China;College of Food Science and Engineering,Jilin Agricultural University,Changchun 130118,China)

机构地区：[1]东北农业大学食品学院,黑龙江哈尔滨150030 [2]吉林农业大学食品科学与工程学院,吉林长春130118

出　　处：《食品科学》2018年第24期54-58,共5页Food Science

基　　金："十三五"国家重点研发计划重点专项(2016YFD0401402)

摘　　要：对不同热处理条件下大豆11S球蛋白的Zeta电位、粒径和红外光谱进行研究。随着热处理时间的延长,80℃和90℃条件下大豆11S球蛋白的Zeta电位绝对值逐渐减小,而100℃条件下Zeta电位绝对值呈先减小后增大的趋势,3个温度条件下11S球蛋白的平均粒径逐渐增加。100℃热处理的Zeta电位绝对值变化更显著,平均粒径更大。Zeta电位和平均粒径的变化与热处理改变了蛋白质的分子结构有关。对于2%的大豆11S球蛋白溶液,80℃热处理过程中β-转角和无规卷曲结构的转化可能相互抵消,而最终表现为α-螺旋结构转变为β-折叠结构;90℃热处理前30 min发生α-螺旋和β-折叠结构向β-转角结构转变,超过30 min各二级结构不再相互转化;100℃热处理前20 min会使α-螺旋和β-折叠结构迅速转变为β-转角和无规卷曲结构,20～45 min各二级结构没有相互转化,而超过45 min后这种转变进一步加强。The zeta potential,particle size and infrared spectroscopic characteristics of 11S glycinin under different heat treatment conditions were investigated.The absolute value of zeta potential was reduced with increasing heat treatment time at 80 or 90℃,while it decreased at first and then increased at 100℃.The average particle size of 11S glycinin was increased at all three temperatures.The absolute value of zeta potential was changed more significantly and the average particle size was larger at 100℃.The changes in zeta potential and average particle size were related to the alteration in the molecular structure of the protein after heat treatment.For 2%11S glycinin solution,the transformation ofβ-turn and random coil structure might offset each other during heat treatment at 80℃,and finallyα-helix was transformed intoβ-sheet structure.Heat treatment at 90℃for 30 min resulted in the transformation ofα-helix andβ-sheet intoβ-turn structure,and the secondary structures were no longer converted to each other after 30 min.In the first 20 min of heat treatment at 100℃,α-helix andβ-sheet were rapidly transformed intoβ-turn and random coil structure,and the secondary structures were not converted to each other from 20 to 45 min of heat treatment.After 45 min,the transformation was further strengthened.

关 键 词：热处理 大豆11S球蛋白 ZETA电位 粒径 红外光谱 

分 类 号：TS201.2[轻工技术与工程—食品科学]