摘要
测定了以葡萄糖酸内酯(GDL)作为凝固剂时不同热处理条件下大豆蛋白主要组分———7S和11S单独胶凝时的流变学曲线,证实了蛋白质的充分变性是GDL引发大豆蛋白胶凝的前提,且已充分热变性的7S和11S组分在单独胶凝时具有大致相当的凝胶强度.通过测定7S和11S组分的物理化学性质,解释了在以GDL作为凝固剂时两组分表现出基本相似的胶凝能力,与7S组分较高的疏水性和11S组分较高的巯基含量有关.
Dynamic viscoelastic properties of soy 7 S and 11 S proteins under different preheating conditions were measured when using GDL as coagulant. The results suggested that full heat denaturation was the precondiction for coagulation of soy protein by GDL, and the strength of denatured 7 S or 11 S gels induced by GDL were about equal. By comparing the physicalchemical properties of 7 S and 11 S globulins, it could be concluded that the similar gelation capacity exhibited when using GDL as the coagulant was due to the high hydrophobicity of 7 S and high -SH content of 11 S.
出处
《无锡轻工大学学报(食品与生物技术)》
CSCD
北大核心
2003年第5期1-4,10,共5页
Journal of Wuxi University of Light Industry
基金
国家自然科学基金项目(20206011)
江苏省自然科学基金项目(BK200269)资助课题.