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超高温热处理对乳蛋白二级结构的影响:傅里叶变换红外光谱分析及潜在致敏活性的见解

Effect of UHT Thermal Treatment on the Secondary Structures of Milk Proteins: Insights From FTIR Analysis and Potential Allergenic Activity.

作者信息

Acuña-Nelson Sergio-Miguel, Henríquez-González Leslie-Patricia, Sepúlveda-Villagra Vieroska-Belén, Opazo-Navarrete Mauricio, Durán-Agüero Samuel, Parra-Flores Julio-Enrique

机构信息

Food Engineering Department University of Bío-Bío, Chillán 3780000, Chile.

Agriaquaculture Nutritional Genomic Center (CGNA), Temuco 4780000, Chile.

出版信息

Int J Food Sci. 2024 Aug 22;2024:1880779. doi: 10.1155/2024/1880779. eCollection 2024.

DOI:10.1155/2024/1880779
PMID:39220440
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11362581/
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. 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. The results suggest that thermal treatments may promote protein aggregation by increasing turns and reducing sheets and helices, which could enhance the allergenic potential of the proteins and facilitate the formation of complexes between different milk proteins, such as -lactoglobulin and -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.

摘要

尽管热处理对牛奶的保存和安全有益,但它们也可能通过影响牛奶的蛋白质成分来改变其免疫原活性。为了获得精确的结果,确定导致食物过敏的特定蛋白质至关重要。因此,研究热处理导致的牛奶蛋白(CMPs)的可能变化是必要的。在本研究中,采用傅里叶变换红外光谱(FTIR)技术分析超高温热处理对牛奶酪蛋白二级结构的影响。利用二阶导数,在1700至1600 cm的酰胺I区域中识别出六个特征峰。结果发现,热处理会使吸收峰发生位移,表明蛋白质构象发生变化,可能过敏活性也发生变化。在样品M8和M9的第一个特征峰(从1621至1600 cm)中清楚地识别出了这些位移。结果表明,热处理可能通过增加β转角并减少β折叠和α螺旋来促进蛋白质聚集,这可能会增强蛋白质的过敏潜力,并促进不同牛奶蛋白(如β-乳球蛋白和β-酪蛋白)之间复合物的形成。由于仅使用一种分析方法(FTIR)来评估蛋白质的二级结构,因此需要进一步的研究来通过实验验证经热处理修饰的蛋白质的过敏活性。

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本文引用的文献

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Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics.
采用核磁共振、傅里叶变换红外光谱和化学计量学分析温度和 pH 值对 β-酪蛋白结构的影响。
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