Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants
The effects of lipid peroxidation on rice bran protein (RBP) structure was examined through Raman Spectroscopy. 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH), acrolein, and malondialdehyde (MDA) are chosen for lipid peroxidation. Incubation of RBP with the increasing concentration of three o...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2022-12-01
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| Series: | CyTA - Journal of Food |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19476337.2022.2107705 |
| _version_ | 1798037065757097984 |
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| author | Linyi Zhou Min Zhang Jieyi Cheng Zhongjiang Wang Zengwang Guo Bailiang Li |
| author_facet | Linyi Zhou Min Zhang Jieyi Cheng Zhongjiang Wang Zengwang Guo Bailiang Li |
| author_sort | Linyi Zhou |
| collection | DOAJ |
| description | The effects of lipid peroxidation on rice bran protein (RBP) structure was examined through Raman Spectroscopy. 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH), acrolein, and malondialdehyde (MDA) are chosen for lipid peroxidation. Incubation of RBP with the increasing concentration of three oxidants resulted in a gradual generation of protein carbonyl derivatives. It can be deduced from the Raman spectra that a low concentration of AAPH and acrolein both decreased the percentage of α-helix and β-sheet, which increased with MDA concentration. The Raman intensities of tryptophan residues of oxidized RBP by AAPH and acrolein, both initially increased and then decreased with oxidation concentration. After MDA treatment, the Raman intensities corresponding to Trp residues and Tyr doublet ratio of RBP were increased and then decreased, and decreased and then increased with oxidation concentration, respectively. The structural change induced by RBP oxidation with the Raman Spectroscopy can aid in refining the function of RBP characteristics and control the adjustment of the storage condition. |
| first_indexed | 2024-04-11T21:21:38Z |
| format | Article |
| id | doaj.art-b9c3a45a91964f378ad553149a64e1f9 |
| institution | Directory Open Access Journal |
| issn | 1947-6337 1947-6345 |
| language | English |
| last_indexed | 2024-04-11T21:21:38Z |
| publishDate | 2022-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | CyTA - Journal of Food |
| spelling | doaj.art-b9c3a45a91964f378ad553149a64e1f92022-12-22T04:02:36ZengTaylor & Francis GroupCyTA - Journal of Food1947-63371947-63452022-12-0120114915710.1080/19476337.2022.2107705Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidantsLinyi Zhou0Min Zhang1Jieyi Cheng2Zhongjiang Wang3Zengwang Guo4Bailiang Li5College of Food Science, Beijing Technology and Business University, Beijing, ChinaCollege of Food Science, Beijing Technology and Business University, Beijing, ChinaCollege of Food Science, Beijing Technology and Business University, Beijing, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang Province, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang Province, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang Province, ChinaThe effects of lipid peroxidation on rice bran protein (RBP) structure was examined through Raman Spectroscopy. 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH), acrolein, and malondialdehyde (MDA) are chosen for lipid peroxidation. Incubation of RBP with the increasing concentration of three oxidants resulted in a gradual generation of protein carbonyl derivatives. It can be deduced from the Raman spectra that a low concentration of AAPH and acrolein both decreased the percentage of α-helix and β-sheet, which increased with MDA concentration. The Raman intensities of tryptophan residues of oxidized RBP by AAPH and acrolein, both initially increased and then decreased with oxidation concentration. After MDA treatment, the Raman intensities corresponding to Trp residues and Tyr doublet ratio of RBP were increased and then decreased, and decreased and then increased with oxidation concentration, respectively. The structural change induced by RBP oxidation with the Raman Spectroscopy can aid in refining the function of RBP characteristics and control the adjustment of the storage condition.https://www.tandfonline.com/doi/10.1080/19476337.2022.2107705Raman Spectroscopystructurerice bran proteinoxidationEspectroscopia Ramanestructura |
| spellingShingle | Linyi Zhou Min Zhang Jieyi Cheng Zhongjiang Wang Zengwang Guo Bailiang Li Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants CyTA - Journal of Food Raman Spectroscopy structure rice bran protein oxidation Espectroscopia Raman estructura |
| title | Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| title_full | Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| title_fullStr | Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| title_full_unstemmed | Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| title_short | Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| title_sort | raman spectroscopy investigate structural change of rice bran protein induced by three oxidants |
| topic | Raman Spectroscopy structure rice bran protein oxidation Espectroscopia Raman estructura |
| url | https://www.tandfonline.com/doi/10.1080/19476337.2022.2107705 |
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