Utilization of ultrasound and glycation to improve functional properties and encapsulated efficiency of proteins in anthocyanins

被引:29
作者
Cui, Huijun [1 ]
Zang, Zhihuan [1 ]
Jiang, Qiao [1 ]
Bao, Yiwen [1 ]
Wu, Yunan [1 ]
Li, Jiaxin [1 ]
Chen, Yi [2 ]
Liu, Xiaoli [3 ]
Yang, Shufang [4 ]
Si, Xu [1 ]
Li, Bin [1 ]
机构
[1] Shenyang Agr Univ, Coll Food Sci, Shenyang 110866, Liaoning, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330031, Jiangxi, Peoples R China
[3] Jiangsu Acad Agr Sci, Inst Agroprod Proc, Nanjing 210014, Jiangsu, Peoples R China
[4] Zhejiang Lanmei Technol Co Ltd, Zhuji 311800, Zhejiang, Peoples R China
基金
中国国家自然科学基金;
关键词
Bovine serum albumin; Casein; Ultrasonic pretreatment; Glycation; Anthocyanins stability; MAILLARD REACTION; PHYSICOCHEMICAL PROPERTIES; ANTIOXIDANT PROPERTIES; ISOLATE; CONJUGATION; DEXTRAN;
D O I
10.1016/j.foodchem.2023.135899
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The purpose of this study is to explore the optimal conditions for the preparation of bovine serum albumin (BSA)/casein (CA)-dextran (DEX) conjugates by ultrasonic pretreatment combined with glycation (U-G treatment). When BSA and CA were treated with ultrasound (40% amplitude, 10 min), the grafting degree increased 10.57% and 6.05%, respectively. Structural analysis revealed that ultrasonic pretreatment changed the secondary structure, further affected functional properties of proteins. After U-G treatment, the solubility and thermal stability of BSA and CA was significantly increased, and the foaming and emulsifying capacity of proteins were also changed. Moreover, ultrasonic pretreatment and glycation exhibited a greater impact on BSA characterized with highly helical structure. Complexes fabricated by U-G-BSA/CA and carboxymethyl cellulose (CMC) exhibited protection on anthocyanins (ACNs), delaying the thermal degradation of ACNs. In conclusion, the protein conjugates treated by ultrasonic pretreatment combined with glycation have excellent functionality and are potential carrier materials.
引用
收藏
页数:12
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