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Comparative effects of phosphorylation and acetylation on glycolysis and myofibrillar proteins degradation in postmortem muscle

文献类型： 外文期刊

作者： Ren, Chi 1 ; Chen, Li 1 ; Bai, Yuqiang 1 ; Hou, Chengli 1 ; Li, Xin 1 ; Schroyen, Martine 2 ; Zhang, Dequan 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Key Lab Agroprod Qual & Safety Harvest Storage Tra, Minist Agr & Rural Affairs, Beijing 100193, Peoples R China

2.Univ Liege, Precis Livestock & Nutr Unit, Gembloux Agrobio Tech, Passage Deportes 2, Gembloux, Belgium

3.Chinese Acad Agr Sci, Inst Food Sci & Technol, 2 Yuanmingyuan West Rd, Beijing 100193, Peoples R China

关键词： Meat; Protein phosphorylation; Protein acetylation; Glycolysis; Protein degradation

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2024 年 257 卷

页码：

收录情况： SCI

摘要： The study investigated the different effects between protein phosphorylation and acetylation on glycolytic enzyme activity and myofibrillar protein degradation. Lamb longissimus thoracis lumborum muscles were homogenized and then inhibitors were added for incubation at 4 C. Phosphatase inhibitor was added to produce a high phosphorylation level (PI group) and lysine deacetylase inhibitor was added to produce a high acetylation level (DI group). The lactate and ATP content in the PI group was inhibited compared with that in the DI group (P < 0.05). Phosphofructokinase (PFK) activity was negatively related with the phosphorylation level and was positively related with the acetylation level in the DI group (P < 0.05). The degradation of troponin T and desmin of the DI group were restrained when compared to that in the PI group (P < 0.05). Compared with initial PFK and desmin, the simulation of phosphorylation and acetylation of PFK and desmin showed different electrostatic potential at the surface and a more unstable structure. The phosphorylation level of the DI group was increased, suggesting that the changes of protein acetylation altered protein phosphorylation. In conclusion, compared with protein phosphorylation, protein acetylation had a greater effect on promoting glycolysis and inhibiting protein degradation.

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