Volume 77, Issue 3 pp. 735-749
Research Article

The influence of the interaction between whey protein and erythritol on protein conformation, interfacial properties and stability

Yumeng Zhang

Yumeng Zhang

College of Food Science, Shenyang Agricultural University, Shenyang, 110866 China

These authors contributed equally to this work.

Contribution: Writing - original draft, Validation, ​Investigation

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Juan Zhang

Juan Zhang

Liaoning Agricultural Development Service Center, Shenyang, 110033 China

These authors contributed equally to this work.

Contribution: Validation, Methodology, ​Investigation

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Junhua Shao

Junhua Shao

College of Food Science, Shenyang Agricultural University, Shenyang, 110866 China

Contribution: Formal analysis

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Mohan Li

Corresponding Author

Mohan Li

College of Food Science, Shenyang Agricultural University, Shenyang, 110866 China

Author for correspondence. E-mail: [email protected]; [email protected]; [email protected]

Contribution: Conceptualization, Project administration, Supervision, Funding acquisition, Writing - original draft, Writing - review & editing

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Xiqing Yue

Corresponding Author

Xiqing Yue

College of Food Science, Shenyang Agricultural University, Shenyang, 110866 China

Author for correspondence. E-mail: [email protected]; [email protected]; [email protected]

Contribution: Conceptualization, Funding acquisition, Writing - review & editing, Project administration, Supervision

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Aijun Xie

Corresponding Author

Aijun Xie

Department of Chemical and Biomolecular Engineering, National University of Singapore, Singapore, 119077 Singapore

Author for correspondence. E-mail: [email protected]; [email protected]; [email protected]

Contribution: Software, Resources, Data curation

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First published: 24 April 2024
Citations: 7

Abstract

This study investigated the impact of erythritol (ERY) on structural and functional properties of whey protein isolate (WPI). FTIR and CD revealed that WPI underwent structural changes, including formation of β-folds and random coils, upon interaction with 20 mg/mL ERY. SEM showed increased surface roughness of WPI, indicating enhanced protein exposure. Moreover, binding rate exceeded 85%, accompanied by increased surface hydrophobicity. Fluorescence spectroscopy indicated a red shift in fluorescence of WPI and tyrosine (Tyr) residues, altering polarity of Tyr environment due to ERY coordination. Additionally, ERY presence enhanced the functional properties of WPI, including foaming, freeze–thaw stability, rheology and antioxidant activity.

CONFLICT OF INTEREST STATEMENT

The authors declare no competing interests.

DATA AVAILABILITY STATEMENT

Data sharing is not applicable to this article as no datasets were generated or analysed during the current study.

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