大豆伴球蛋白组成亚基热稳定性及其相关影响因素分析  

Heat stability and surface properties of the constituent subunits of soy β-conglycinin

作　　者：黄科礼[1] 袁德保[1] 郑恒光[2] 杨晓泉[1] 顾炜[1] 

机构地区：[1]华南理工大学轻工与食品学院,广东广州510641 [2]福建省农业科学院农业工程技术研究所,福建福州350003

出　　处：《食品工业科技》2011年第6期169-171,225,共4页Science and Technology of Food Industry

基　　金：国家自然科学基金(20776050);广东省自然科学基金(7006508);教育部高校博士点基金(20070561059)

摘　　要：为了明确大豆伴球蛋白良好热稳定性的根源,以大豆伴球蛋白及其组成亚基为研究对象,从组分的角度分析探讨了表面疏水性和表面电荷对热稳定性的影响,探求热稳定性与表面性质之间的关系。实验结果表明,在低离子强度下,三种亚基都具有良好的热稳定性,粒度分布显示,β亚基生成的聚集体最大,达到100nm;在高离子强度下,三种亚基的粒度分布皆呈增大趋势,β亚基增幅最大,致使部分β亚基絮凝沉淀;大豆伴球蛋白亚基组分的热稳定性与表面疏水性及Zeta-电位有紧密的关系,通过直接控制三者的热聚集行为,从而影响体系的热稳定性。In order to find out the different contributions of the constituent subunits of soy β-conglycinin on its heat stability,their roles were studied,then the relationship of hydrophobicity and Zeta-potential vs their heat stability were explored.The results showed that,each subunit owned excellent heat stability under the low ironic strength.And β subunit exhibited the largest aggregates among the samples（about 100nm in diameter）from the particle distribution.Under the high ironic strength,the particle size of subunit the subunits increased after heat treatment.The particle size of β subunit increased markedly and precipitates could be seen in its solution.The heat stability of the subunits was decided by the surface properties of the constituent subunits directly through controlling the thermal aggregation of the subunits.

关 键 词：大豆伴球蛋白 亚基 热稳定性 表面疏水性 Zeta-电位 

分 类 号：TS201.2[轻工技术与工程—食品科学]