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dc.contributor.author Acuña-Nelson, Sergio Miguel
dc.contributor.author Henríquez-González, Leslie Patricia
dc.contributor.author Sepúlveda-Villagra, Vieroska Belén
dc.contributor.author Opazo-Navarrete, Mauricio
dc.contributor.author Durán-Agüero, Samuel
dc.contributor.author Parra-Flores, Julio Enrique
dc.date.accessioned 2026-02-08T03:23:41Z
dc.date.available 2026-02-08T03:23:41Z
dc.date.issued 2024
dc.identifier.issn 2356-7015
dc.identifier.uri https://repositorio.uss.cl/handle/uss/20271
dc.description Publisher Copyright: © 2024 Sergio-Miguel Acuña-Nelson et al.
dc.description.abstract 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. en
dc.language.iso eng
dc.relation.ispartof vol. 2024 Issue: Pages:
dc.source International Journal of Food Science
dc.title Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins : Insights from FTIR Analysis and Potential Allergenic Activity en
dc.type Artículo
dc.identifier.doi 10.1155/2024/1880779
dc.publisher.department Facultad de Ciencias de la Rehabilitación y Calidad de Vida


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