Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
The aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decreas...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-11-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/22/6799 |
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| author | Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis |
| author_facet | Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis |
| author_sort | Hilal Yılmaz |
| collection | DOAJ |
| description | The aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decrease of fluorescence intensity of BLG at all pH conditions when BLG was mixed with PGM rather than with BSM. We propose that, unlike BSM, the tertiary structure of PGM changes and the hydrophobic regions are exposed at pH 3 due to protonation of negatively charged residues. Results suggest that PGM also facilitated the structural unfolding of BLG and its binding with PGM by a hydrophobic interaction, especially at acidic pH, which was further supported by extrinsic fluorescence spectroscopy. Hydrophobic interaction is suggested as the dominant interaction mechanism between BLG and PGM at pH 3, whereas electrostatic interaction is the dominant one between BLG and BSM. |
| first_indexed | 2024-03-10T05:15:19Z |
| format | Article |
| id | doaj.art-f454a5be06334fe7b9e4a877df77cde6 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T05:15:19Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-f454a5be06334fe7b9e4a877df77cde62023-11-23T00:33:54ZengMDPI AGMolecules1420-30492021-11-012622679910.3390/molecules26226799Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence SpectroscopyHilal Yılmaz0Seunghwan Lee1Ioannis S. Chronakis2Department of Biotechnology, Bartın University, Kutlubey Campus, Bartın 74100, TurkeyDepartment of Mechanical Engineering, Technical University of Denmark, DK-2800 Kgs. Lyngby, DenmarkDTU-Food, Technical University of Denmark, Kemitorvet, B202, DK-2800 Kgs. Lyngby, DenmarkThe aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decrease of fluorescence intensity of BLG at all pH conditions when BLG was mixed with PGM rather than with BSM. We propose that, unlike BSM, the tertiary structure of PGM changes and the hydrophobic regions are exposed at pH 3 due to protonation of negatively charged residues. Results suggest that PGM also facilitated the structural unfolding of BLG and its binding with PGM by a hydrophobic interaction, especially at acidic pH, which was further supported by extrinsic fluorescence spectroscopy. Hydrophobic interaction is suggested as the dominant interaction mechanism between BLG and PGM at pH 3, whereas electrostatic interaction is the dominant one between BLG and BSM.https://www.mdpi.com/1420-3049/26/22/6799fluorescenceβ-lactoglobulinbovine submaxillary mucinporcine gastric mucinpH |
| spellingShingle | Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy Molecules fluorescence β-lactoglobulin bovine submaxillary mucin porcine gastric mucin pH |
| title | Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy |
| title_full | Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy |
| title_fullStr | Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy |
| title_full_unstemmed | Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy |
| title_short | Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy |
| title_sort | interactions of β lactoglobulin with bovine submaxillary mucin vs porcine gastric mucin the role of hydrophobic and hydrophilic residues as studied by fluorescence spectroscopy |
| topic | fluorescence β-lactoglobulin bovine submaxillary mucin porcine gastric mucin pH |
| url | https://www.mdpi.com/1420-3049/26/22/6799 |
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