Literature DB >> 35636156

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

Yichang Wang1, Bailiang Li2, Yanan Guo3, Caihua Liu4, Jun Liu5, Bin Tan6, Zengwang Guo7, Zhongjiang Wang8, Lianzhou Jiang9.   

Abstract

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 β1-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 β1-sheets, β2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-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 α-helix and β-turn contents, surface hydrophobicity and absolute ζ-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.
Copyright © 2022 The Author(s). Published by Elsevier B.V. All rights reserved.

Entities:  

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

Mesh:

Substances:

Year:  2022        PMID: 35636156      PMCID: PMC9149199          DOI: 10.1016/j.ultsonch.2022.106046

Source DB:  PubMed          Journal:  Ultrason Sonochem        ISSN: 1350-4177            Impact factor:   9.336


  21 in total

1.  A validated bioanalytical method in mouse, rat, rabbit and human plasma for the quantification of one of the steroid glycosides found in Hoodia gordonii extract.

Authors:  Weijun Wang; Paul J Russell; Graeme T Clark; Derek Lewis; Kun Nang Cheng
Journal:  Food Chem Toxicol       Date:  2010-08-25       Impact factor: 6.023

Review 2.  Flocculation of protein-stabilized oil-in-water emulsions.

Authors:  Eric Dickinson
Journal:  Colloids Surf B Biointerfaces       Date:  2010-07-07       Impact factor: 5.268

3.  Effect of thermal treatment on interfacial properties of beta-lactoglobulin.

Authors:  Dennis A Kim; Michel Cornec; Ganesan Narsimhan
Journal:  J Colloid Interface Sci       Date:  2005-05-01       Impact factor: 8.128

4.  Structural and functional changes in ultrasonicated bovine serum albumin solutions.

Authors:  Ibrahim Gülseren; Demet Güzey; Barry D Bruce; Jochen Weiss
Journal:  Ultrason Sonochem       Date:  2006-09-07       Impact factor: 7.491

5.  Structural changes of native milk proteins subjected to controlled shearing and heating.

Authors:  Anushka Mediwaththe; Dimuthu Bogahawaththa; Manpreet Kaur Grewal; Jayani Chandrapala; Todor Vasiljevic
Journal:  Food Res Int       Date:  2018-08-03       Impact factor: 6.475

6.  Characterization of heat-stable whey protein: Impact of ultrasound on rheological, thermal, structural and morphological properties.

Authors:  Anju Boora Khatkar; Amarjeet Kaur; Sunil Kumar Khatkar; Nitin Mehta
Journal:  Ultrason Sonochem       Date:  2018-08-27       Impact factor: 7.491

7.  Effects of ultrasound pre-treatment on the structure of β-conglycinin and glycinin and the antioxidant activity of their hydrolysates.

Authors:  Yuting Wang; Zhongjiang Wang; Cíntia Ladeira Handa; Jing Xu
Journal:  Food Chem       Date:  2016-09-12       Impact factor: 7.514

8.  Formation of soy protein isolate (SPI)-citrus pectin (CP) electrostatic complexes under a high-intensity ultrasonic field: Linking the enhanced emulsifying properties to physicochemical and structural properties.

Authors:  Xiaobin Ma; Tianyi Yan; Furong Hou; Weijun Chen; Song Miao; Donghong Liu
Journal:  Ultrason Sonochem       Date:  2019-08-23       Impact factor: 7.491

9.  Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments.

Authors:  Shanshan Jiang; Junzhou Ding; Juan Andrade; Taha M Rababah; Ali Almajwal; Mahmoud M Abulmeaty; Hao Feng
Journal:  Ultrason Sonochem       Date:  2017-03-28       Impact factor: 7.491

10.  Effects of ultrasound-assisted vacuum tumbling on the oxidation and physicochemical properties of pork myofibrillar proteins.

Authors:  Ruyu Zhang; Lujuan Xing; Dacheng Kang; Lei Zhou; Lin Wang; Wangang Zhang
Journal:  Ultrason Sonochem       Date:  2021-05-04       Impact factor: 7.491

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