4.7 Article

Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates

期刊

ULTRASONICS SONOCHEMISTRY
卷 87, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.ultsonch.2022.106046

关键词

Soybean protein; Oxidized aggregates; Structure; Emulsifying properties; Interfacial properties; Ultrasonic treatment

资金

  1. National Key RD Program [2021YFD2100400]
  2. Heilongjiang Province Hundred, Thousand, Ten Thousand Engineering Science and Technology Major Project [2021ZX12B02]
  3. Shandong key R&D plan (major scientific and technological innovation project) [2022CXGC010603]
  4. Youth Talent Promotion Project [2019QNRC001]
  5. Heilongjiang Province Major Achievements Transformation Project [CG19A002]
  6. Major industrial key projects for the transformation of new and old kinetic energy in Shandong Province

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Oxidative attack leads to the weakening of soybean protein's structure and functionality, while ultrasonic treatment can improve the emulsifying and interfacial features of the protein.
Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with beta 1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of beta 1-sheets, beta 2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute zeta-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The alpha-helix and beta-turn contents, surface hydrophobicity and absolute zeta-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein.

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