Formation of amyloid fibrils from soy protein hydrolysate: Effects of selective proteolysis on β-conglycinin

被引:82
作者
Xia, Wenjie [1 ,2 ]
Zhang, Han [3 ]
Chen, Jingyao [2 ]
Hu, Hao [1 ,2 ]
Rasulov, Farruhbek [1 ,2 ]
Bi, Dingren [4 ]
Huang, Xingjian [1 ,2 ]
Pan, Siyi [1 ,2 ]
机构
[1] Huazhong Agr Univ, Minist Educ, Key Lab Environm Correlat Dietol, Wuhan 430070, Peoples R China
[2] Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China
[3] RMIT Univ, Sch Appl Sci, Melbourne, Vic 3001, Australia
[4] Huazhong Agr Univ, Coll Anim Sci & Technol, Wuhan 430070, Peoples R China
基金
中国国家自然科学基金;
关键词
Selective proteolysis; Soy protein; Amyloid fibril; beta-Conglycinin; SUBUNIT COMPOSITION; IONIC-STRENGTH; THIOFLAVIN-T; PROCESSING CONDITIONS; STORAGE PROTEIN; GLYCININ; PH; ISOLATE; AGGREGATION; SOLUBILITY;
D O I
10.1016/j.foodres.2017.08.059
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The soy protein hydrolysate subjected to selective proteolysis on beta-conglycinin (referred to as D beta H, contrast group) and a control soy protein isolate sample without addition of protease (referred to as CSPI, blank group) were adopted as experimental samples. By employing the "subtraction" mode of logical thinking, we aimed to compare the differences between CSPI and D beta H on fibrillation at pH 2.0 with heating at 95 degrees C. The results showed when heated for 60 min, CSPI tended to form short worm-like fibrils while D beta H long semiflexible fibrils. When heating time was prolonged to 360 min, the fibrils formed from them both exhibited cluster. Whereas when heated for 720 min, no fibrillar aggregates appeared from them. This study would help explore the effects of beta-conglycinin on the fibril formation of soy protein isolate by a new way.
引用
收藏
页码:268 / 276
页数:9
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