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Covalent modification of soy protein isolate by (-)-epigallocatechin-3-gallate: effects on structural and emulsifying properties
被引:47
|作者:
Tao, Fei
[1
]
Jiang, He
[2
]
Chen, Wenwei
[3
]
Zhang, Yongyong
[3
]
Pan, Jiarong
[3
]
Jiang, Jiaxin
[3
]
Jia, Zhenbao
[3
]
机构:
[1] China Jiliang Univ, Coll Standardizat, Hangzhou, Zhejiang, Peoples R China
[2] Hangzhou Inst Food & Drug Control, Ctr Food Safety & Qual, Hangzhou, Zhejiang, Peoples R China
[3] China Jiliang Univ, Key Lab Marine Food Qual & Hazard Controlling Tec, Hangzhou, Zhejiang, Peoples R China
基金:
中国国家自然科学基金;
关键词:
soy protein isolate;
(-)-Epigallocatechin-3-gallate;
covalent modification;
emulsifying property;
IN-WATER EMULSIONS;
MICROBIAL TRANSGLUTAMINASE;
SURFACE-PROPERTIES;
PHENOLIC-COMPOUNDS;
CROSS-LINKING;
HYDROPHOBICITY;
AGGREGATION;
FLAVONOIDS;
PRESSURE;
BINDING;
D O I:
10.1002/jsfa.9114
中图分类号:
S [农业科学];
学科分类号:
09 ;
摘要:
BACKGROUND Soy protein isolate (SPI) has promising applications in various food products because of its excellent functional properties and nutritional quality. The structural and emulsifying properties of covalently modified SPI by (-)-epigallocatechin-3-gallate (EGCG) were investigated. RESULTS CONCLUSION SPI was covalently modified by EGCG under alkaline conditions. SDS-PAGE analysis revealed that EGCG modification caused crosslinking of SPI proteins. Circular dichroism spectra demonstrated that the secondary structure of SPI proteins was changed by EGCG modification. In addition, the modifications resulted in the perturbation of the tertiary structure of SPI as evidenced by intrinsic fluorescence spectra and surface hydrophobicity measurements. Oil-in-water emulsions of modified SPI had smaller droplet sizes and better creaming stability compared to those from unmodified SPI. The covalent modification by EGCG improved the emulsifying property of SPI. This study therefore provided an innovative approach for improving the emulsifying properties of proteins. (c) 2018 Society of Chemical Industry
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页码:5683 / 5689
页数:7
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