Collagen is the most abundant fibrous protein in animal's body and is widely used for biomedical and pharmaceutical applications. The principal sources of this protein are bovine, porcine and fish skin and bones. In Colombia, bovine bones are waste from meat industry, this material have potential as an alternative source of collagen isolation. The aim of this study was to evaluate the composition and some properties of type I collagen (COL I) extracted of bovine bones of Zebu-Bos Primigenius Indicus and its use as textile finishing to modify two types of fabrics: first a taffeta weave and the second a single jersey knit, both 100% cotton. The extracted bone collagen showed the main characteristic bands of this material in the FTIR spectra, corresponding to amide A, I, II and III. Gel electrophoresis (SDS-PAGE) presented the main bands of α1 and α2 chains characteristic of COL I with a molecular weight of approximately 120 kDa and the amino acid profile of hydrolyzed protein evaluated by amino acid analysis showed 9.4% of hydroxyproline, 10.3% proline and 16.9% of glycine content. Two traditional methods of applying finished textiles were evaluated to modify both fabrics with COL I, exhibiting better attachment through PAD method compared with exhaustion method. These results suggest that bone is an alternative source for type I collagen extraction, which can be applied as a functional textile finishing for traditional fabrics for implementation in healthtech field.