Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy
The color stability of anthocyanins (ACN) has been shown to be improved by interaction with whey proteins (WP). In this study, we explore the ACN–WP interaction using Fourier transform infrared spectroscopy (IR). ACN from purple corn, grape, and black carrot (50 μM) were evaluated. IR spectra (4000–...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/27/5/1538 |
| _version_ | 1827651097787891712 |
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| author | Shuai Ren Luis Rodriguez-Saona M. Monica Giusti |
| author_facet | Shuai Ren Luis Rodriguez-Saona M. Monica Giusti |
| author_sort | Shuai Ren |
| collection | DOAJ |
| description | The color stability of anthocyanins (ACN) has been shown to be improved by interaction with whey proteins (WP). In this study, we explore the ACN–WP interaction using Fourier transform infrared spectroscopy (IR). ACN from purple corn, grape, and black carrot (50 μM) were evaluated. IR spectra (4000–700 cm<sup>−1</sup>) were collected for native and preheated (40–80 °C) WP (5 mg/mL) and ACN–WP mixtures at pH 7.4. Soft independent modeling of class analogy was used to analyze the IR data. The WP secondary structure changed after heat treatments and after interaction with ACN. As expected, the WP α-helices decreased, and β-sheet increased after heat treatment. The intensities of the WP amide I and II bands decreased after ACN addition, revealing a decrease in the WP α-helix content. Higher preheating temperatures (70–80 °C) resulted in a more disordered WP structure that favored stronger WP–ACN interactions related to amide III changes. Addition of ACN stabilized WP structure due to heat denaturation, but different ACN structures had different binding affinities with WP. WP structure had less change after interaction with ACN with simpler structures. These results increase our understanding of ACN–WP interactions, providing a potential strategy to extend anthocyanin color stability by WP addition. |
| first_indexed | 2024-03-09T20:30:05Z |
| format | Article |
| id | doaj.art-66ad368692e24559a66a2011726ea5ff |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T20:30:05Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-66ad368692e24559a66a2011726ea5ff2023-11-23T23:25:54ZengMDPI AGMolecules1420-30492022-02-01275153810.3390/molecules27051538Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared SpectroscopyShuai Ren0Luis Rodriguez-Saona1M. Monica Giusti2Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Road, Columbus, OH 43210, USADepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Road, Columbus, OH 43210, USADepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Road, Columbus, OH 43210, USAThe color stability of anthocyanins (ACN) has been shown to be improved by interaction with whey proteins (WP). In this study, we explore the ACN–WP interaction using Fourier transform infrared spectroscopy (IR). ACN from purple corn, grape, and black carrot (50 μM) were evaluated. IR spectra (4000–700 cm<sup>−1</sup>) were collected for native and preheated (40–80 °C) WP (5 mg/mL) and ACN–WP mixtures at pH 7.4. Soft independent modeling of class analogy was used to analyze the IR data. The WP secondary structure changed after heat treatments and after interaction with ACN. As expected, the WP α-helices decreased, and β-sheet increased after heat treatment. The intensities of the WP amide I and II bands decreased after ACN addition, revealing a decrease in the WP α-helix content. Higher preheating temperatures (70–80 °C) resulted in a more disordered WP structure that favored stronger WP–ACN interactions related to amide III changes. Addition of ACN stabilized WP structure due to heat denaturation, but different ACN structures had different binding affinities with WP. WP structure had less change after interaction with ACN with simpler structures. These results increase our understanding of ACN–WP interactions, providing a potential strategy to extend anthocyanin color stability by WP addition.https://www.mdpi.com/1420-3049/27/5/1538IRstructure changeanthocyanin–whey protein interactionheat denaturesoft independent modeling of class analogy |
| spellingShingle | Shuai Ren Luis Rodriguez-Saona M. Monica Giusti Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy Molecules IR structure change anthocyanin–whey protein interaction heat denature soft independent modeling of class analogy |
| title | Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy |
| title_full | Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy |
| title_fullStr | Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy |
| title_full_unstemmed | Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy |
| title_short | Analyzing the Interaction between Anthocyanins and Native or Heat-Treated Whey Proteins Using Infrared Spectroscopy |
| title_sort | analyzing the interaction between anthocyanins and native or heat treated whey proteins using infrared spectroscopy |
| topic | IR structure change anthocyanin–whey protein interaction heat denature soft independent modeling of class analogy |
| url | https://www.mdpi.com/1420-3049/27/5/1538 |
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