Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications
The study aimed to assess the oxidative modification behavior of bovine myofibrillar proteins (MPs) cysteines (Cys) by hydroxyl radical (·OH) through the construction of an in vitr Fenton reaction system. The ·OH generated by the Fenton reaction induced large-scale oxidative modification of Cys, and...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-01-01
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| Series: | Food Chemistry: X |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157524010344 |
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| author | Jiale Li Jun Liu Hui Yue Yuanyuan Ma He Li Yuanliang Hu Xiang Yu Weiwei Dong Yanli Feng |
| author_facet | Jiale Li Jun Liu Hui Yue Yuanyuan Ma He Li Yuanliang Hu Xiang Yu Weiwei Dong Yanli Feng |
| author_sort | Jiale Li |
| collection | DOAJ |
| description | The study aimed to assess the oxidative modification behavior of bovine myofibrillar proteins (MPs) cysteines (Cys) by hydroxyl radical (·OH) through the construction of an in vitr Fenton reaction system. The ·OH generated by the Fenton reaction induced large-scale oxidative modification of Cys, and redox proteomics identified a total of 1192 differential oxidation sites (Dos), 59 Dos were located in the MPs structure. The Cys of actin (17 Dos), myosin/myomesin (16 Dos), tenascin (12 Dos) and sarcomere (10 Dos) in the MPs structure showed active oxidative modification behavior towards ·OH, especially with the “-C-X-X-X-X-W-” structure amino acid sequence showed high sensitivity. Notably, the oxidative modification of Cys by ·OH was an irreversible process, as evidenced mainly by a significant decrease (p < 0.05) in protein sulfhydryl groups and unfolding of protein secondary and tertiary structures. While the intermolecular forces of MPs were altered, with the most direct result being the degradation of MPs, which had a positive effect on beef tenderness and a negative effect on water-holding capacity. |
| format | Article |
| id | doaj-art-d2fbd609d1d94b6fb49513ee37786f8a |
| institution | Kabale University |
| issn | 2590-1575 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj-art-d2fbd609d1d94b6fb49513ee37786f8a2025-02-12T05:32:12ZengElsevierFood Chemistry: X2590-15752025-01-0125102146Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modificationsJiale Li0Jun Liu1Hui Yue2Yuanyuan Ma3He Li4Yuanliang Hu5Xiang Yu6Weiwei Dong7Yanli Feng8Hubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, China; Hubei Engineering Research Center of Special Wild Vegetables Breeding and Comprehensive Utilization Technology, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, China; Hubei Engineering Research Center of Special Wild Vegetables Breeding and Comprehensive Utilization Technology, Hubei Normal University, Huangshi 435002, China; Corresponding author at: No.11, Cihu Road, Huangshi City 435002, Hubei Province, China.Hubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, China; Hubei Engineering Research Center of Special Wild Vegetables Breeding and Comprehensive Utilization Technology, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, China; Hubei Engineering Research Center of Special Wild Vegetables Breeding and Comprehensive Utilization Technology, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, ChinaHubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, ChinaThe study aimed to assess the oxidative modification behavior of bovine myofibrillar proteins (MPs) cysteines (Cys) by hydroxyl radical (·OH) through the construction of an in vitr Fenton reaction system. The ·OH generated by the Fenton reaction induced large-scale oxidative modification of Cys, and redox proteomics identified a total of 1192 differential oxidation sites (Dos), 59 Dos were located in the MPs structure. The Cys of actin (17 Dos), myosin/myomesin (16 Dos), tenascin (12 Dos) and sarcomere (10 Dos) in the MPs structure showed active oxidative modification behavior towards ·OH, especially with the “-C-X-X-X-X-W-” structure amino acid sequence showed high sensitivity. Notably, the oxidative modification of Cys by ·OH was an irreversible process, as evidenced mainly by a significant decrease (p < 0.05) in protein sulfhydryl groups and unfolding of protein secondary and tertiary structures. While the intermolecular forces of MPs were altered, with the most direct result being the degradation of MPs, which had a positive effect on beef tenderness and a negative effect on water-holding capacity.http://www.sciencedirect.com/science/article/pii/S2590157524010344Hydroxyl radicalMyofibrillar proteinsDegradationRedox proteomicsCysteine sites |
| spellingShingle | Jiale Li Jun Liu Hui Yue Yuanyuan Ma He Li Yuanliang Hu Xiang Yu Weiwei Dong Yanli Feng Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications Food Chemistry: X Hydroxyl radical Myofibrillar proteins Degradation Redox proteomics Cysteine sites |
| title | Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| title_full | Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| title_fullStr | Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| title_full_unstemmed | Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| title_short | Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| title_sort | elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications |
| topic | Hydroxyl radical Myofibrillar proteins Degradation Redox proteomics Cysteine sites |
| url | http://www.sciencedirect.com/science/article/pii/S2590157524010344 |
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