Combination of pulsed electric field and pH shifting improves the solubility, emulsifying, foaming of commercial soy protein isolate

被引:93
|
作者
Wang, Rui [1 ,3 ]
Wang, Lang-Hong [1 ,2 ]
Wen, Qing-Hui [1 ,3 ,4 ]
He, Fei [1 ,3 ]
Xu, Fei-Yue [1 ,3 ]
Chen, Bo-Ru [1 ,3 ]
Zeng, Xin-An [1 ,2 ,3 ]
机构
[1] South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510641, Guangdong, Peoples R China
[2] Foshan Univ, Guangdong Key Lab Food Intelligent Mfg, Foshan 528225, Peoples R China
[3] Overseas Expertise Intro Ctr Discipline Innovat F, Guangzhou 510641, Guangdong, Peoples R China
[4] Univ Melbourne, Sch Chem, Parkville, Vic 3010, Australia
基金
中国国家自然科学基金;
关键词
Soy protein isolate; Pulsed electric field; pH shifting; Modification; FUNCTIONAL-PROPERTIES; STRUCTURAL-PROPERTIES; PHYSICOCHEMICAL PROPERTIES; SURFACE-PROPERTIES; STABILITY; ACID; FLEXIBILITY; EXTRACTION; FRACTIONS; OXIDATION;
D O I
10.1016/j.foodhyd.2022.108049
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
In this study, the effects of a new dual modification method, pulsed electric field (PEF) and pH shifting treatment, on the solubility, emulsifying and foaming properties of commercial soy protein isolate (SPI) were investigated. Results showed that the combination of PEF and pH shifting treatment, particularly at moderate PEF strength (10 kV/cm) and alkaline conditions (pH 11), facilitated protein structure unfolding and formation of smaller aggregates, substantially enhancing the solubility of SPI from 26.06% to 70.34%. Higher flexibility, surface hydrophobicity, and free sulfhydryl content were also found in the modified SPI, which boosted interfacial ac-tivity and significantly enhanced emulsifying and foaming properties. In alkaline environments, the enhanced functional properties of SPI at moderate PEF strength may be attributed to the appropriate oxidation of proteins by free radicals produced by electrochemical processes and the additional unfolding of protein conformations by polarization. The functional characteristics of SPI were decreased by an increase in PEF strength (20 kV/cm), which may be due to the tendency of the protein to aggregate and undergo excessive oxidation. This work may provide an effective methodological and theoretical basis for the modification of SPI by combining PEF and pH shifting treatment.
引用
收藏
页数:13
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