热诱导菜豆属7S球蛋白纤维聚集研究.pdfVIP

现代食品科技 Modern Food Science and Technology 2012, Vol.28, No.11 热诱导菜豆属7S 球蛋白纤维聚集研究 刘晶，唐传核 （华南理工大学轻工与食品学院，广东广州510640） 摘要：研究了菜豆属球蛋白(芸豆和绿豆)在低pH 低离子强度条件下热诱导形成的自组装纤维聚集机理。通过对制备的球蛋白进 行热性质及临界形成凝胶浓度分析，选定85 ℃和0.5%作为自组装纤维化的参数。通过硫代黄色素T(Th T)荧光法，动态光散射(DLS) 和原子力显微镜（AFM ）表征蛋白纤维化聚集程度及形态。结果表明：芸豆和绿豆球蛋白的Th T 最大荧光强度在1h 之内剧烈增大 （分别是765 和 1093），表明芸豆和绿豆球蛋白自组装纤维化的“构筑单元”主要产生于加热的起始阶段。DLS 结果显示芸豆自组装纤 维聚集的能力比绿豆强。但是二者的自组装机理有所不同。AFM 图清晰地显示了芸豆球蛋白在加热12 h 时自组装形成规则的高度有 序的“念珠串状”长线性纤维，绿豆则形成无规则的短棒状纤维和大量碎片状纤维。这为研究进一步研究超低固形物下基于自组装技术 的纤维型植物蛋白凝胶的制备提供参考。 关键词：菜豆属球蛋白；纤维聚集；自组装；淀粉样纤维；原子力显微镜 文章篇号：1673-9078(2012)11-1450-1453 Heat-Induced Fibrillar Aggregation of 7S Globulins (vicilins) from Phaseolus Legumes LIU Jing, TANG Chuan-he (College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China) Abstract: The heat -induced fibrillar aggregations of 7S Globulins (vicilins) from kidney bean (Gk) and mung bean (Gm) at low pH and low ionic strength were characterized using dynamic light scattering (DLS), Thioflavin T (Th T) fluorescence assay and atomic force microscopy (AFM). According to thermal characteristics and phase diagram analysis, 85 °C and 0.5% were chosen as denaturation temperature and proper protein concentration . Results also showed that heating led to fibrillar aggregation. Th T maximum fluorescence intensity of Gk and Gm increased dramatically to 765 and 1093 within one hour, indicating that the building blocks were formed at the initial heating periods. DLS data suggested Gk exhibited stronger ability of self assembly and fibrillar aggregation. However, the extent of aggregation and morphology of formed fibrils varied distinctly. AFM data displayed clearly that Gk