College of Food and Bioengineering, Xihua University, Chengdu, Sichuan 610039, China; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Food Res Int. 2023 Oct;172:113126. doi: 10.1016/j.foodres.2023.113126. Epub 2023 Jun 12.
This work aimed to investigate the effects of heat treatments at different temperatures (60, 70 and 90 °C, expressed as HT-60, HT-70 and HT-90) on interfacial composition and protein-lipid co-oxidation in whey protein isolate (WPI)-stabilised O/W emulsions during storage. Compared with control group, all heated emulsions exhibited weaker physical stability over 10 days of storage, which verified by the increased droplet size, as well as decreased adsorbed protein levels and absolute ζ-potential values. Moreover, proteins recovered from the HT-90 emulsion showed the highest fluorescence intensity and red-shift of the maximum emission wavelength, indicating partial unfolding of the protein structure. Meanwhile, severe changes in protein structure were also observed in the HT-70 and HT-90 emulsions, which clearly verified by the degradation of bovine serum albumin, α-lactalbumin and β-lactoglobulin. Furthermore, HT-70 and HT-90 emulsions showed lower levels of lipid hydroperoxides and thiobarbituric acid reactive substances. In contrast, the recovered proteins were subject to severe oxidative stress as indicated by carbonyl and N'-formyl-L-kynurenine. Hierarchical cluster and correlation analysis implied that the process of protein-lipid co-oxidation is inevitable, but it can be retarded by heat treatment. Our results clearly revealed the relevance among heat treatment, interfacial adsorption property, and the protein-lipid co-oxidation of O/W emulsions.
本研究旨在探究不同温度(60、70 和 90°C,分别表示为 HT-60、HT-70 和 HT-90)的热处理对乳清蛋白分离物(WPI)稳定的 O/W 乳液在贮藏过程中界面组成和蛋白-脂协同氧化的影响。与对照组相比,所有加热的乳液在贮藏 10 天内表现出较弱的物理稳定性,这可以通过增加的粒径、吸附蛋白水平和绝对 ζ-电位值的降低来验证。此外,从 HT-90 乳液中回收的蛋白质表现出最高的荧光强度和最大发射波长的红移,表明蛋白质结构的部分展开。同时,在 HT-70 和 HT-90 乳液中也观察到蛋白质结构的严重变化,这可以通过牛血清白蛋白、α-乳白蛋白和β-乳球蛋白的降解清楚地验证。此外,HT-70 和 HT-90 乳液中的脂质过氧化物和硫代巴比妥酸反应物质水平较低。相比之下,回收的蛋白质受到严重的氧化应激,如羰基和 N'-甲酰基-L-犬尿氨酸所示。层次聚类和相关分析表明,蛋白质-脂协同氧化的过程是不可避免的,但可以通过热处理来延迟。我们的结果清楚地揭示了热处理、界面吸附特性和 O/W 乳液中蛋白质-脂协同氧化之间的相关性。