Protein Phosphorylation Induced by Pyruvate Kinase M2 Inhibited Myofibrillar Protein Degradation in Post-Mortem Muscle

文献类型： 外文期刊

第一作者： Ren, Chi

作者： Ren, Chi;Song, Xubo;Dong, Yu;Hou, Chengli;Chen, Li;Wang, Zhenyu;Li, Xin;Zhang, Dequan;Ren, Chi;Schroyen, Martine

作者机构：

关键词： meat; tenderness; myofibrillar protein degradation; protein phosphorylation; pyruvate kinase

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.1； 五年影响因子：6.3 ）

ISSN： 0021-8561

年卷期： 2023 年 71 卷 41 期

页码：

收录情况： SCI

摘要： Myofibrillar protein degradation is primarily related to meat tenderness through protein phosphorylation regulation. Pyruvate kinase M2 (PKM2), a glycolytic rate-limiting enzyme, is also regarded as a protein kinase to catalyze phosphorylation. The objective of this study was to investigate the relationship between myofibrillar protein degradation and phosphorylation induced by PKM2. Myofibrillar proteins were incubated with PKM2 at 4, 25, and 37 degrees C. The global phosphorylation level of myofibrillar proteins in the PKM2 group was significantly increased, but it was sensitive to temperature (P < 0.05). Compared with 4 and 25 degrees C, PKM2 significantly increased the myofibrillar protein phosphorylation level from 0.5 to 6 h at 37 degrees C (P < 0.05). In addition, the degradation of desmin and actin was inhibited after they were phosphorylated by PKM2 when incubated at 37 degrees C. These results demonstrate that phosphorylation of myofibrillar proteins catalyzed by PKM2 inhibited protein degradation and provided a possible pathway for meat tenderization through glycolytic enzyme regulation.

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