Effect of titin phosphorylation on degradation of titin from skeletal muscles
The degradation of titin could make the myofibrillar fragmentation to improve meat tenderization during postmortem. This study aimed to investigate effect of phosphorylation on titin degradation. Protein kinase A (PKA) and alkaline phosphatase (AP) were added to crude titin extracted from ovine long...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2023-07-01
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| Series: | Food Science and Human Wellness |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453022002208 |
| _version_ | 1797710286416773120 |
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| author | Ying Wang Xin Li Dequan Zhang Zheng Li Baocai Xu Jie Zhu |
| author_facet | Ying Wang Xin Li Dequan Zhang Zheng Li Baocai Xu Jie Zhu |
| author_sort | Ying Wang |
| collection | DOAJ |
| description | The degradation of titin could make the myofibrillar fragmentation to improve meat tenderization during postmortem. This study aimed to investigate effect of phosphorylation on titin degradation. Protein kinase A (PKA) and alkaline phosphatase (AP) were added to crude titin extracted from ovine longissimus lumborum (LL) muscles. Phosphorylated/dephosphorylated titin were incubated with μ-calpain at 4 °C for 2 days. Results showed titin in AP group started degradation earlier than that in PKA and control groups. There were 20, 16 and 12 phosphorylated sites identified by iTRAQ in the PKA, control and AP group, respectively. 3D structure of dephosphorylated titin fragment was simulated and its molecular dynamics trajectory analysis was performed using Discovery StudioTM. The dihedral angle in AP group was less and the dephosphorylated fragment had a higher kinetic energy and total energy. We suggested that changes caused by AP treatment might make titin unstable, which easily degraded by μ-calpain. |
| first_indexed | 2024-03-12T06:49:58Z |
| format | Article |
| id | doaj.art-2e1fe2071c714de7ad32654aea91dc16 |
| institution | Directory Open Access Journal |
| issn | 2213-4530 |
| language | English |
| last_indexed | 2024-03-12T06:49:58Z |
| publishDate | 2023-07-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj.art-2e1fe2071c714de7ad32654aea91dc162023-09-03T00:18:36ZengTsinghua University PressFood Science and Human Wellness2213-45302023-07-0112411841191Effect of titin phosphorylation on degradation of titin from skeletal musclesYing Wang0Xin Li1Dequan Zhang2Zheng Li3Baocai Xu4Jie Zhu5Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; School of Food Science and Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei University of Technology, Hefei 230000, China; Laboratory of Biomechanics and Engineering, Institute of Biophysics and College of Science, Northwest A&F University, Yangling 712100, ChinaKey Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaKey Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Correspondence author at: Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China. Fax: +86-10-62819392.Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaSchool of Food Science and Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei University of Technology, Hefei 230000, ChinaLaboratory of Biomechanics and Engineering, Institute of Biophysics and College of Science, Northwest A&F University, Yangling 712100, ChinaThe degradation of titin could make the myofibrillar fragmentation to improve meat tenderization during postmortem. This study aimed to investigate effect of phosphorylation on titin degradation. Protein kinase A (PKA) and alkaline phosphatase (AP) were added to crude titin extracted from ovine longissimus lumborum (LL) muscles. Phosphorylated/dephosphorylated titin were incubated with μ-calpain at 4 °C for 2 days. Results showed titin in AP group started degradation earlier than that in PKA and control groups. There were 20, 16 and 12 phosphorylated sites identified by iTRAQ in the PKA, control and AP group, respectively. 3D structure of dephosphorylated titin fragment was simulated and its molecular dynamics trajectory analysis was performed using Discovery StudioTM. The dihedral angle in AP group was less and the dephosphorylated fragment had a higher kinetic energy and total energy. We suggested that changes caused by AP treatment might make titin unstable, which easily degraded by μ-calpain.http://www.sciencedirect.com/science/article/pii/S2213453022002208MeatTitinDegradationPhosphorylationAlkaline phosphatase |
| spellingShingle | Ying Wang Xin Li Dequan Zhang Zheng Li Baocai Xu Jie Zhu Effect of titin phosphorylation on degradation of titin from skeletal muscles Food Science and Human Wellness Meat Titin Degradation Phosphorylation Alkaline phosphatase |
| title | Effect of titin phosphorylation on degradation of titin from skeletal muscles |
| title_full | Effect of titin phosphorylation on degradation of titin from skeletal muscles |
| title_fullStr | Effect of titin phosphorylation on degradation of titin from skeletal muscles |
| title_full_unstemmed | Effect of titin phosphorylation on degradation of titin from skeletal muscles |
| title_short | Effect of titin phosphorylation on degradation of titin from skeletal muscles |
| title_sort | effect of titin phosphorylation on degradation of titin from skeletal muscles |
| topic | Meat Titin Degradation Phosphorylation Alkaline phosphatase |
| url | http://www.sciencedirect.com/science/article/pii/S2213453022002208 |
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