Improved encapsulation effect and structural properties of whey protein isolate by dielectric barrier discharge cold plasma

被引：8
作者：
Xu, Ting [1 ]
Li, Xiaojing [1 ,2 ]
Wu, Caie [1 ,2 ]
Fan, Gongjian [1 ,2 ]
Li, Tingting [1 ,2 ]
Zhou, Dandan [1 ,2 ]
Zhu, Jinpeng [1 ]
Wu, Zhihao [1 ]
Hua, Xiaowen [3 ]
机构：
[1] Nanjing Forestry Univ, Coll Light Ind & Food Engn, Nanjing 210037, Jiangsu, Peoples R China
[2] Nanjing Forestry Univ, Coinnovat Ctr Efficient Proc & Utilizat Forest Res, Nanjing 210037, Peoples R China
[3] Chinese Acad Sci, Cixi Inst Biomed Engn, Ningbo Inst Mat Technol & Engn, Ningbo 315201, Peoples R China
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2024年 / 257卷
关键词：
Whey protein isolate; Atmospheric cold plasma; Encapsulation; BETA-LACTOGLOBULIN; PHYSICOCHEMICAL PROPERTIES; MILK-PROTEINS; HIGH-PRESSURE; SOY PROTEIN; BINDING; SPECTROSCOPY; AGGREGATION; BEHAVIOR; ZEIN;
D O I：
10.1016/j.ijbiomac.2023.128556
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The whey protein isolate (WPI) was modified by dielectric barrier discharge cold plasma (DBD) in order to improve its encapsulation efficiency of rutin. In this work, the effect of DBD treatment on structure and physicochemical properties of WPI and the interaction between DBD-treated WPI and rutin were investigated. The results showed that the structural change of WPI leaded to the exposure of internal hydrophobic groups, increasing the interaction site with rutin. The encapsulation efficiency of DBD-treated WPI (30 kV, 30 s) on rutin was improved by 12.42 % compared with control group. The results of multispectral analysis showed that static quenching occurred in the process of interaction between DBD-treated and rutin, hydrogen bond and van der Waals force were the main forces between them. Therefore, DBD treatment can be used as a method to improve the encapsulation efficiency of WPI on hydrophobic active substances.
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页数：11
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