Characterization of Type I and Type III Collagen in the Intramuscular Connective Tissue of Wuzhumuqin Sheep

Simple Summary Collagen is an important component of muscle tissue that maintains muscle structure and also contributes to meat quality. However, the characteristics of intramuscular connective tissue (IMCT) collagen of Wuzhumuqin sheep are unknown. The purpose of this study was to analyze the characteristics of IMCT collagen in Wuzhumuqin sheep at different growth stages and to determine the correlation between them. The results showed that collagen-related genes were highly expressed at 9 and 12 months of age. The amino acid content, solubility, thermal stability, and degree of cross-linking of collagen were altered by collagen type, muscle type, and age. Multiple patterns of correlation between collagen characteristics are essential for the development of IMCT. These findings will contribute to a better understanding of the relationship between the characteristics of collagen, and also provide a theoretical basis for further studies on the impacts of collagen on meat quality. Intramuscular connective tissue (IMCT) collagen is an important factor in meat quality. This study analyzed the characteristics of type I and III collagen in the IMCT of the semitendinosus (SD) and longissimus dorsi (LD) of Wuzhumuqin sheep at different growth stages (6, 9, 12, and 18 months). Utilizing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR), collagen types I and III were successfully isolated and shown to contain an intact triple helix structure. Immunofluorescence revealed that these collagens were located in the endomysium and perimysium. Collagen-related genes were significantly expressed in sheep aged 9 and 12 months. The amino acid content increased with age in type I collagen whereas it decreased in type III collagen. Furthermore, type III collagen contained more hydroxyproline (Hyd) than type I collagen. Differential scanning calorimetry (DSC) revealed that the thermal stability of collagen increased with age, accompanied by a decrease in solubility. Semitendinosus muscle had more collagen cross-linkages than LD muscle due to the high pyridinoline (Pyr) content in the endomysium. Finally, a correlation analysis highlighted the multiple correlations between characteristics in different types of collagen during sheep growth. In summary, the collagen characteristics in the IMCT of sheep were impacted by collagen type, muscle type, and age. Furthermore, the various correlations between these characteristics may play an important role in the development of IMCT.