The beef market is constantly growing, and as a result, more residues are generated daily. The organic matter from these wastes contributes to the deterioration of the environmental because of its high polluting potential. The use of these by-products, such as bovine tendons, for the extraction of collagen is a viable alternative for increasing the value of the raw material and contributing to the sustainability of the food industry. The objective of this study was to characterize the collagen extracted from bovine tendons by physicochemical analysis (moisture, protein and infrared spectrometry - FTIR) and to compare it with the commercial fiber powder sample provided by NovaProm Food Ingredients. The results showed that both the commercial collagen powder and the extracted sample presented similar values for water content (9.84% and 8.95%, respectively). The protein content found for the extracted sample was 77.64%, whereas the commercial sample had a content of 88.56%. The FTIR analysis of the collagen samples presented the main bands characteristic of the stretching of the C-N bond and N-H vibration at 1239 cm-1. These vibrations are sensitive to changes in the secondary structure of the tropocolagen (triple helix). The absorption at 1446 cm-1 corresponds to pyrrolidine ring vibrations of proline and hydroxyproline. Its intensity is independent of the structural variations of the collagen matrix. The comparison of the characteristic bands in the spectra of collagen and the results for the protein and moisture analyses with those cited in the literature and those of the commercial sample indicated that the collagen had been extracted, the triple helix was preserved in the extraction process (essential for the gelling), and no denaturation of the collagen occurred.