| Autor: |
Yang RQ; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China., Chen YL; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.; Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China., Lin D; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.; Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China., Cao KY; Department of Biological Sciences, National University of Singapore, Singapore 117558, Singapore., Sun LC; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.; Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China., Zhang LJ; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.; Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China., Yoshida A; Graduate School of Fisheries and Environmental Sciences, Nagasaki University, Nagasaki 852-8521, Japan., Cao MJ; College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.; Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China. |
| Abstrakt: |
Matrix metalloproteinases (MMPs) play critical roles in the degradation of collagens, while their mechanism remains unclear. In the present study, the involvement of matrix metalloproteinases (MMPs) in collagen degradation of sea bass muscle during cold storage was explored. Immunohistochemical staining results showed significant degradation of type I collagen in the connective tissue of muscle endomysium during cold storage, thus affecting the muscle structural integrity and quality. Western blot analysis revealed an increment in the α1 chain and a decrease in the β and γ chains of type I collagen. Immunofluorescence staining showed that MMP-2, MMP-9, and MMP-13 were distributed in the endomysium surrounding the muscle fibers. Additionally, the catalytic domains of MMP-2, MMP-9, and MMP-13 with biological activities were successfully expressed. The degradation trend of type I collagen by MMPs under 4 °C was similar to that of muscle collagen during cold storage, suggesting that the degradation of type I collagen was attributed to the cooperative action of the MMPs. In conclusion, our study elucidated that the MMPs-engaged degradation of type I collagen is quite possibly the leading cause of sea bass muscle softening during cold storage. |
