Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity
Although thermal treatments are beneficial for the preservation and safety of milk, they can also alter its immunogenic activity by affecting its protein components. To achieve precise results, it is essential to identify the specific proteins that cause food allergies. Therefore, investigating the...
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| Format: | Article |
| Language: | English |
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Wiley
2024-01-01
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| Series: | International Journal of Food Science |
| Online Access: | http://dx.doi.org/10.1155/2024/1880779 |
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| author | Sergio-Miguel Acuña-Nelson Leslie-Patricia Henríquez-González Vieroska-Belén Sepúlveda-Villagra Mauricio Opazo-Navarrete Samuel Durán-Agüero Julio-Enrique Parra-Flores |
| author_facet | Sergio-Miguel Acuña-Nelson Leslie-Patricia Henríquez-González Vieroska-Belén Sepúlveda-Villagra Mauricio Opazo-Navarrete Samuel Durán-Agüero Julio-Enrique Parra-Flores |
| author_sort | Sergio-Miguel Acuña-Nelson |
| collection | DOAJ |
| description | Although thermal treatments are beneficial for the preservation and safety of milk, they can also alter its immunogenic activity by affecting its protein components. To achieve precise results, it is essential to identify the specific proteins that cause food allergies. Therefore, investigating the possible alterations of cow’s milk proteins (CMPs) resulting from thermal treatments is necessary. In this study, the Fourier transform infrared spectroscopy (FTIR) technique was used to analyze the effect of UHT thermal treatment on the secondary structures of milk casein. Using the second derivative, six characteristic peaks were identified in the Amide I region, ranging from 1700 to 1600 cm−1. It was found that thermal treatments produce shifts in absorption peaks, indicating changes in protein conformation and possibly in allergenic activity. These shifts were clearly identified in the first characteristic peak of samples M8 and M9, from 1621 to 1600 cm−1. The results suggest that thermal treatments may promote protein aggregation by increasing β turns and reducing β sheets and α helices, which could enhance the allergenic potential of the proteins and facilitate the formation of complexes between different milk proteins, such as β-lactoglobulin and κ-casein. Further studies are needed to experimentally validate the allergenic activity of proteins modified by thermal treatments, as only an analytical method (FTIR) was used to evaluate the secondary structures of the proteins. |
| format | Article |
| id | doaj-art-cc5013440b58482db6837aa61ca9198e |
| institution | Kabale University |
| issn | 2314-5765 |
| language | English |
| publishDate | 2024-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Food Science |
| spelling | doaj-art-cc5013440b58482db6837aa61ca9198e2025-02-03T11:30:42ZengWileyInternational Journal of Food Science2314-57652024-01-01202410.1155/2024/1880779Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic ActivitySergio-Miguel Acuña-Nelson0Leslie-Patricia Henríquez-González1Vieroska-Belén Sepúlveda-Villagra2Mauricio Opazo-Navarrete3Samuel Durán-Agüero4Julio-Enrique Parra-Flores5Food Engineering DepartmentFood Engineering DepartmentFood Engineering DepartmentAgriaquaculture Nutritional Genomic Center (CGNA)Nutrition and Dietetic SchoolNutrition and Public Health DepartmentAlthough thermal treatments are beneficial for the preservation and safety of milk, they can also alter its immunogenic activity by affecting its protein components. To achieve precise results, it is essential to identify the specific proteins that cause food allergies. Therefore, investigating the possible alterations of cow’s milk proteins (CMPs) resulting from thermal treatments is necessary. In this study, the Fourier transform infrared spectroscopy (FTIR) technique was used to analyze the effect of UHT thermal treatment on the secondary structures of milk casein. Using the second derivative, six characteristic peaks were identified in the Amide I region, ranging from 1700 to 1600 cm−1. It was found that thermal treatments produce shifts in absorption peaks, indicating changes in protein conformation and possibly in allergenic activity. These shifts were clearly identified in the first characteristic peak of samples M8 and M9, from 1621 to 1600 cm−1. The results suggest that thermal treatments may promote protein aggregation by increasing β turns and reducing β sheets and α helices, which could enhance the allergenic potential of the proteins and facilitate the formation of complexes between different milk proteins, such as β-lactoglobulin and κ-casein. Further studies are needed to experimentally validate the allergenic activity of proteins modified by thermal treatments, as only an analytical method (FTIR) was used to evaluate the secondary structures of the proteins.http://dx.doi.org/10.1155/2024/1880779 |
| spellingShingle | Sergio-Miguel Acuña-Nelson Leslie-Patricia Henríquez-González Vieroska-Belén Sepúlveda-Villagra Mauricio Opazo-Navarrete Samuel Durán-Agüero Julio-Enrique Parra-Flores Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity International Journal of Food Science |
| title | Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity |
| title_full | Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity |
| title_fullStr | Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity |
| title_full_unstemmed | Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity |
| title_short | Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity |
| title_sort | effect of uht thermal treatment on the secondary structures of milk proteins insights from ftir analysis and potential allergenic activity |
| url | http://dx.doi.org/10.1155/2024/1880779 |
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