Inhibition or improvement for acidic subunits fibril aggregation formation from β-conglycinin, glycinin and basic subunits

被引：22
作者：
Dong, Shi-Rong [1 ]
Xu, Hong-Hua [1 ]
Li, Bo-Yang [1 ]
Cheng, Wen [1 ]
Zhang, Li-Gang [1 ]
机构：
[1] Northeast Agr Univ, Minist Educ, Coll Food, Harbin 150030, Peoples R China
来源：
JOURNAL OF CEREAL SCIENCE | 2016年 / 70卷
基金：
中国国家自然科学基金;
关键词：
Acidic subunits; Glycinin; Basic subunits; Fibril aggregates; AMYLOID-LIKE FIBRILS; WHEY-PROTEIN; SOY PROTEINS; LACTOGLOBULIN; KINETICS; HEAT; MILK; FOOD;
D O I：
10.1016/j.jcs.2016.07.002
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
It was difficult to form nice nano-fibril structure from glycinin, but in this study, we found a new method to solve the problem. The acidic subunits isolated from glycinin could form thinner, longer and more flexible fibril aggregation compared with glycinin or beta-conglycinin fibril aggregation at pH2.0 and 95 degrees C after heating 20 h beta-Conglycinin, glycinin and basic subunits were respectively mixed with acidic subunits heating at 95 beta C and pH2.0 to gain insight into the influence on the formation of acidic subunits fibrils. The different soy proteins interaction was probably the main reasons for inhibition or improvement the acidic subunits fibrils formation. The morphology and kinetics of fibril formation and the change of secondary structure were analyzed by transmission electron microscopy (TEM), fluorescent dye Thioflavin T (Th T) and far-UV circular dichroism (CD) spectroscopy. These results showed that beta-conglycinin improved but glycinin and its basic subunits inhibited or destroyed the formation of acidic subunits fibrils. Glycinin and its basic subunits with higher surface hydrophobicity produced more aggregation, and fast aggregate was disastrous for the formation of acidic subunits fibrils. Furthermore, CD results indicated that basic subunits probably inhibited the alpha-helix transition into beta-strands of acidic subunits. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码：263 / 269
页数：7
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