Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development
Since the initial findings that food tannin/salivary protein interaction and subsequent precipitation is the main cause of the astringency development, numerous studies have concentrated on the supramolecular characterization of these bindings. Most of these works have focused on the low-molecular-w...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/13/6/862 |
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| author | Elvira Manjón Ignacio García-Estévez María Teresa Escribano-Bailón |
| author_facet | Elvira Manjón Ignacio García-Estévez María Teresa Escribano-Bailón |
| author_sort | Elvira Manjón |
| collection | DOAJ |
| description | Since the initial findings that food tannin/salivary protein interaction and subsequent precipitation is the main cause of the astringency development, numerous studies have concentrated on the supramolecular characterization of these bindings. Most of these works have focused on the low-molecular-weight salivary proteins, in particular proline-rich proteins, hardly considering the involvement of the high-molecular-weight salivary proteins (HMW<sub>SPs</sub>). Herein, different techniques such as fluorescence quenching, Isothermal Titration Calorimetry and HPLC-MS-DAD were employed to determine the occurrence of molecular interactions between three HMW<sub>SPs</sub>, namely, mucin, α-amylase and albumin, and a complex extract of tannins composed mainly of flavan-3-ols. The obtained results prove the capability of the three HMW<sub>SPs</sub> to effectively interact with the flavan-3-ol extract, involving different forces and action mechanisms. Flavan-3-ols are capable of interacting with mucins by a mechanism that includes the formation of stable ground-state complexes that led to approximately 90% flavan-3-ol precipitation, while for albumin and α-amylase, the interaction model of a “sphere of action” was established, which represented only 20% flavan-3-ol precipitation. These data highlight the relevance of including HMW<sub>SPs</sub> in astringency analyses, paying special heed to the role of mucins in the interaction and subsequent precipitation of dietary tannins. |
| first_indexed | 2024-04-24T18:16:33Z |
| format | Article |
| id | doaj.art-14036a53964e4035a502aaef5e94e760 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-04-24T18:16:33Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-14036a53964e4035a502aaef5e94e7602024-03-27T13:41:01ZengMDPI AGFoods2304-81582024-03-0113686210.3390/foods13060862Possible Role of High-Molecular-Weight Salivary Proteins in Astringency DevelopmentElvira Manjón0Ignacio García-Estévez1María Teresa Escribano-Bailón2Department of Analytical Chemistry, Nutrition and Food Science, Universidad de Salamanca, E37007 Salamanca, SpainDepartment of Analytical Chemistry, Nutrition and Food Science, Universidad de Salamanca, E37007 Salamanca, SpainDepartment of Analytical Chemistry, Nutrition and Food Science, Universidad de Salamanca, E37007 Salamanca, SpainSince the initial findings that food tannin/salivary protein interaction and subsequent precipitation is the main cause of the astringency development, numerous studies have concentrated on the supramolecular characterization of these bindings. Most of these works have focused on the low-molecular-weight salivary proteins, in particular proline-rich proteins, hardly considering the involvement of the high-molecular-weight salivary proteins (HMW<sub>SPs</sub>). Herein, different techniques such as fluorescence quenching, Isothermal Titration Calorimetry and HPLC-MS-DAD were employed to determine the occurrence of molecular interactions between three HMW<sub>SPs</sub>, namely, mucin, α-amylase and albumin, and a complex extract of tannins composed mainly of flavan-3-ols. The obtained results prove the capability of the three HMW<sub>SPs</sub> to effectively interact with the flavan-3-ol extract, involving different forces and action mechanisms. Flavan-3-ols are capable of interacting with mucins by a mechanism that includes the formation of stable ground-state complexes that led to approximately 90% flavan-3-ol precipitation, while for albumin and α-amylase, the interaction model of a “sphere of action” was established, which represented only 20% flavan-3-ol precipitation. These data highlight the relevance of including HMW<sub>SPs</sub> in astringency analyses, paying special heed to the role of mucins in the interaction and subsequent precipitation of dietary tannins.https://www.mdpi.com/2304-8158/13/6/862α-amylasemucinhuman serum albuminfood flavan-3-olsmolecular interactions |
| spellingShingle | Elvira Manjón Ignacio García-Estévez María Teresa Escribano-Bailón Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development Foods α-amylase mucin human serum albumin food flavan-3-ols molecular interactions |
| title | Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development |
| title_full | Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development |
| title_fullStr | Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development |
| title_full_unstemmed | Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development |
| title_short | Possible Role of High-Molecular-Weight Salivary Proteins in Astringency Development |
| title_sort | possible role of high molecular weight salivary proteins in astringency development |
| topic | α-amylase mucin human serum albumin food flavan-3-ols molecular interactions |
| url | https://www.mdpi.com/2304-8158/13/6/862 |
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