Correlation between surface hydrophobicity changes and surface activity changes of soybean protein isolates caused by structural changes


Citation

Tu, J. L. and Li, J. S. and Huang, G. X. and Yan, L. J. (2024) Correlation between surface hydrophobicity changes and surface activity changes of soybean protein isolates caused by structural changes. International Food Research Journal (Malaysia), 31. pp. 952-957. ISSN 2231 7546

Abstract

The present work aimed to examine the association between the changes in the surface hydrophobicity and surface activity of soybean protein isolate (SPI) following structural alterations. To this end, the effects of heating, pH modification, ultrasonication, surfactant (SDS, sodium dodecyl sulphate) treatment, alkaline protease hydrolysis, peracetic acid treatment, and acylation on the surface activity and surface hydrophobicity of SPI were investigated. The results demonstrated that the changes in the surface hydrophobicity of SPI could accurately reflect the changes in its surface activity. A strong correlation between surface hydrophobicity and surface activity alterations was noted after the SPI molecules underwent structural modifications. The higher the surface hydrophobicity of the treated SPI, the greater its surface activity. Given that the surface hydrophobicity of SPI reflects the actual distribution of hydrophobic residues on its surface, this parameter can serve as a key indicator for evaluating and predicting changes in the surface activity of SPI.


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Abstract

The present work aimed to examine the association between the changes in the surface hydrophobicity and surface activity of soybean protein isolate (SPI) following structural alterations. To this end, the effects of heating, pH modification, ultrasonication, surfactant (SDS, sodium dodecyl sulphate) treatment, alkaline protease hydrolysis, peracetic acid treatment, and acylation on the surface activity and surface hydrophobicity of SPI were investigated. The results demonstrated that the changes in the surface hydrophobicity of SPI could accurately reflect the changes in its surface activity. A strong correlation between surface hydrophobicity and surface activity alterations was noted after the SPI molecules underwent structural modifications. The higher the surface hydrophobicity of the treated SPI, the greater its surface activity. Given that the surface hydrophobicity of SPI reflects the actual distribution of hydrophobic residues on its surface, this parameter can serve as a key indicator for evaluating and predicting changes in the surface activity of SPI.

Additional Metadata

[error in script]
Item Type: Article
AGROVOC Term: protein isolates
AGROVOC Term: heating
AGROVOC Term: surfactants
AGROVOC Term: acylation
AGROVOC Term: correlation
AGROVOC Term: soybeans
AGROVOC Term: surfactants
Geographical Term: China
Depositing User: Nor Hasnita Abdul Samat
Date Deposited: 18 Mar 2026 06:41
Last Modified: 18 Mar 2026 06:41
URI: http://webagris.upm.edu.my/id/eprint/3135

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