Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein
(1) Background: The effects of protein oxidization induced by malondialdehyde (MDA), which was selected as a representative of lipid peroxidation products, on the structure and functional properties of walnut protein were investigated. (2) Methods: Walnut protein isolate was produced by alkali-solub...
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| Format: | Article |
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MDPI AG
2022-08-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/16/2432 |
| _version_ | 1797432166649430016 |
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| author | Lingge Sun Qingzhi Wu Xiaoying Mao |
| author_facet | Lingge Sun Qingzhi Wu Xiaoying Mao |
| author_sort | Lingge Sun |
| collection | DOAJ |
| description | (1) Background: The effects of protein oxidization induced by malondialdehyde (MDA), which was selected as a representative of lipid peroxidation products, on the structure and functional properties of walnut protein were investigated. (2) Methods: Walnut protein isolate was produced by alkali-soluble acid precipitation. The modification of walnut protein isolate was conducted by MDA solutions (0, 0.01, 0.1, 1, and 10 Mm), which were incubated in the dark for 24 h. (3) Results: Increased carbonyl content and the degradation of sulfhydryl groups indicated MDA-induced protein oxidization. The circular dichroism spectra revealed disruption of the ordered protein secondary structure. The change in the tertiary conformation of the MDA-treated protein was observed through intrinsic fluorescence. Small polypeptide chain scission was observed at low MDA concentrations (≤0.1 mM) and protein aggregation was observed at high MDA concentrations (>0.1 mM) using high-performance size exclusion chromatography. Oxidized protein solubility was reduced. Furthermore, the emulsification stability index, foam capacity, and foam stability of walnut proteins were increased after treatment with 0.1 mM of MDA. An excessive concentration of MDA (>0.1 mM) decreased emulsification and foaming properties. (4) Conclusions: These results show that MDA oxidation modified the structure of walnut protein and further affected its function, which should be taken into account in processing walnut protein products. |
| first_indexed | 2024-03-09T09:57:22Z |
| format | Article |
| id | doaj.art-6d7f022c94764670a01ce58f4606e64c |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T09:57:22Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-6d7f022c94764670a01ce58f4606e64c2023-12-01T23:42:23ZengMDPI AGFoods2304-81582022-08-011116243210.3390/foods11162432Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut ProteinLingge Sun0Qingzhi Wu1Xiaoying Mao2School of Food Science and Technology, Shihezi University, Shihezi 832000, ChinaSchool of Food Science and Technology, Shihezi University, Shihezi 832000, ChinaSchool of Food Science and Technology, Shihezi University, Shihezi 832000, China(1) Background: The effects of protein oxidization induced by malondialdehyde (MDA), which was selected as a representative of lipid peroxidation products, on the structure and functional properties of walnut protein were investigated. (2) Methods: Walnut protein isolate was produced by alkali-soluble acid precipitation. The modification of walnut protein isolate was conducted by MDA solutions (0, 0.01, 0.1, 1, and 10 Mm), which were incubated in the dark for 24 h. (3) Results: Increased carbonyl content and the degradation of sulfhydryl groups indicated MDA-induced protein oxidization. The circular dichroism spectra revealed disruption of the ordered protein secondary structure. The change in the tertiary conformation of the MDA-treated protein was observed through intrinsic fluorescence. Small polypeptide chain scission was observed at low MDA concentrations (≤0.1 mM) and protein aggregation was observed at high MDA concentrations (>0.1 mM) using high-performance size exclusion chromatography. Oxidized protein solubility was reduced. Furthermore, the emulsification stability index, foam capacity, and foam stability of walnut proteins were increased after treatment with 0.1 mM of MDA. An excessive concentration of MDA (>0.1 mM) decreased emulsification and foaming properties. (4) Conclusions: These results show that MDA oxidation modified the structure of walnut protein and further affected its function, which should be taken into account in processing walnut protein products.https://www.mdpi.com/2304-8158/11/16/2432MDAprotein oxidationstructurefunctional properties |
| spellingShingle | Lingge Sun Qingzhi Wu Xiaoying Mao Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein Foods MDA protein oxidation structure functional properties |
| title | Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein |
| title_full | Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein |
| title_fullStr | Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein |
| title_full_unstemmed | Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein |
| title_short | Effects of Oxidation Modification by Malondialdehyde on the Structure and Functional Properties of Walnut Protein |
| title_sort | effects of oxidation modification by malondialdehyde on the structure and functional properties of walnut protein |
| topic | MDA protein oxidation structure functional properties |
| url | https://www.mdpi.com/2304-8158/11/16/2432 |
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