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Driving forces of disaggregation and reaggregation of peanut protein isolates in aqueous dispersion induced by high-pressure microfluidization

文献类型： 外文期刊

作者： Gong, Kuijie 1 ; Chen, Lirong 1 ; Xia, Haiyong 1 ; Dai, Hongcui 1 ; Li, Xiaoyue 1 ; Sun, Linlin 1 ; Kong, Weilin 1 ; Liu, 1 ;

作者机构： 1.Shandong Acad Agr Sci, Crop Res Inst, Jinan 250100, Shandong, Peoples R China

关键词： Peanut protein isolate; High-pressure microfluidization; Driving forces

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2019 年 130 卷

页码：

收录情况： SCI

摘要： Our previous report described that high-pressure microfluidization (HPM) treatment can disaggregate peanut protein isolates (PPIs) to prepare antihypertensive peptide fractions. In the present study, we investigated the driving forces of disaggregation and reaggregation of PPIs in aqueous dispersion induced by HPM treatment and discussed the mechanism. The driving forces of hydrogen bonds, surface hydrophobicity, sulfhydryl/disulfide bonds (SH/SS) and zeta-potential, which are responsible for disaggregation and reaggregation, were studied. HPM treatment changed the polar environment and promoted surface hydrophobicity and the formation of disulfide bonds (SS), while the free sulfhydryl (SH) group content was decreased. The magnitude of the zeta-potential and beta-sheet content increased when the pressure was <= 120 MPa. However, the magnitude of those values decreased when the pressure was >120 MPa. Hydrophobic interactions, SH/SS interchange reactions, hydrogen bonds and electrostatic interactions cannot individually induce changes in PPIs. Combination of the applied forces drove the disaggregation and reaggregation of PPIs in aqueous dispersion. (C) 2019 Published by Elsevier B.V.

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