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Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability
[Display omitted] •Ultrasound combined with pH-shifting could improve the secondary and tertiary structure of 7S.•pH12-shifting combined with ultrasound (U-7S-12) resulted in more significant protein changes than pH2-shifting combined with ultrasound (U-7S-2).•Ultrasound combined with pH-shifting en...
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Published in: | Ultrasonics sonochemistry 2022-11, Vol.90, p.106186-106186, Article 106186 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Ultrasound combined with pH-shifting could improve the secondary and tertiary structure of 7S.•pH12-shifting combined with ultrasound (U-7S-12) resulted in more significant protein changes than pH2-shifting combined with ultrasound (U-7S-2).•Ultrasound combined with pH-shifting enhanced the emulsifying properties and stabilityof 7S.
This present work underlines the effect of pH-shifting at pH 2 and pH 12 individually or combined with ultrasound treatment to modify the molecular structure of β-conglycinin (7S) on its emulsifying properties and stability. Fourier transform infrared (FTIR) spectroscopy and intrinsic fluorescence spectroscopy showed that pH-shifting improves the molecular structure of 7S, while ultrasound further promotes structural changes. In particular, the pH-shifting at pH 12 combined with ultrasound treatment (U-7S-12) resulted in more significant changes than the pH-shifting at pH 2 combined with ultrasound (U-7S-2). U-7S-12 showed a significant reduction in protein particle size from 152 to 34.77 nm and a relatively smooth protein surface compared to 7S. The protein had the highest surface hydrophobicity and flexibility at 81,560.0 and 0.45, respectively, and the free sulfhydryl content from 1.57 to 2.02 μmol/g. In addition, we characterized the emulsions prepared after 7S treatment. The single or combined treatment increased the interfacial protein adsorption of the samples, which showed lower viscosity and shear stress compared to 7S. The U-7S-12 emulsion exhibited the highest emulsifying properties and was more stable than other emulsions under creaming, heating, and freeze–thaw conditions. In summary, the concerted action of pH-shifting and ultrasound can modify the structure, and combined alkaline pH-shifting and ultrasound treatment can further improve the emulsifying properties and stability of 7S. |
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ISSN: | 1350-4177 1873-2828 |
DOI: | 10.1016/j.ultsonch.2022.106186 |