Effect of heat treatment on the physical stability, interfacial composition and protein-lipid co-oxidation of whey protein isolate-stabilised O/W emulsions
[Display omitted] •Heat treatment decreased the physical stability of O/W emulsions.•Increasing temperature alter the structure of adsorbed and unadsorbed proteins.•Interfacial composition degraded with increasing temperature.•Heat treatment retarded the protein-lipid co-oxidation of O/W emulsions....
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| Published in | Food research international Vol. 172; p. 113126 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Elsevier Ltd
01.10.2023
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| Subjects | |
| Online Access | Get full text |
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| Abstract | [Display omitted]
•Heat treatment decreased the physical stability of O/W emulsions.•Increasing temperature alter the structure of adsorbed and unadsorbed proteins.•Interfacial composition degraded with increasing temperature.•Heat treatment retarded the protein-lipid co-oxidation of O/W emulsions.
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. |
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| AbstractList | [Display omitted]
•Heat treatment decreased the physical stability of O/W emulsions.•Increasing temperature alter the structure of adsorbed and unadsorbed proteins.•Interfacial composition degraded with increasing temperature.•Heat treatment retarded the protein-lipid co-oxidation of O/W emulsions.
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. 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. 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.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. |
| ArticleNumber | 113126 |
| Author | Chen, Jiaxin Liu, Qian Wang, Hui Zhao, Zihan He, Junjie Li, Xin Tang, Jie |
| Author_xml | – sequence: 1 givenname: Jiaxin surname: Chen fullname: Chen, Jiaxin organization: College of Food and Bioengineering, Xihua University, Chengdu, Sichuan 610039, China – sequence: 2 givenname: Junjie surname: He fullname: He, Junjie organization: College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China – sequence: 3 givenname: Zihan surname: Zhao fullname: Zhao, Zihan organization: College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China – sequence: 4 givenname: Xin surname: Li fullname: Li, Xin organization: Sharable Platform of Large-Scale Instruments & Equipments, Northeast Agricultural University, Harbin, Heilongjiang 150030, China – sequence: 5 givenname: Jie surname: Tang fullname: Tang, Jie organization: College of Food and Bioengineering, Xihua University, Chengdu, Sichuan 610039, China – sequence: 6 givenname: Qian surname: Liu fullname: Liu, Qian email: liuqian@neau.edu.cn organization: College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China – sequence: 7 givenname: Hui surname: Wang fullname: Wang, Hui email: huiwang@neau.edu.cn organization: College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China |
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•Heat treatment decreased the physical stability of O/W emulsions.•Increasing temperature alter the structure of adsorbed and unadsorbed... 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... |
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| SubjectTerms | adsorption bovine serum albumin Co-oxidation behaviour droplet size emulsions fluorescence food research heat Heat treatment Interfacial composition lipid peroxides Microstructure Oil-in-water emulsion oxidative stress protein structure wavelengths whey protein isolate |
| Title | Effect of heat treatment on the physical stability, interfacial composition and protein-lipid co-oxidation of whey protein isolate-stabilised O/W emulsions |
| URI | https://dx.doi.org/10.1016/j.foodres.2023.113126 https://www.proquest.com/docview/2863293020 https://www.proquest.com/docview/3153161746 |
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