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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 C.;Chen L.;Bai Y.;Hou C.;Li X.;Schroyen M.;Zhang D.

作者机构：

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

期刊名称： International Journal of Biological Macromolecules

ISSN： 0141-8130

年卷期： 2024 年 257 卷

页码：

收录情况： SCIE（2024版） ; ; EI（2024版）

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. © 2023 Elsevier B.V.

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