Functional textile finishing of type I collagen isolated from bovine bone for potential healthtech
- PMID: 30891510
- PMCID: PMC6389544
- DOI: 10.1016/j.heliyon.2019.e01260
Functional textile finishing of type I collagen isolated from bovine bone for potential healthtech
Abstract
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.
Keywords: Materials science.
Figures






References
-
- Pati F., Adhikari B., Dhara S. Isolation and characterization of fish scale collagen of higher thermal stability. Bioresour. Technol. 2010;101(10):3737–3742. - PubMed
-
- Bailey A.J., Paul R.G., Knott L. Mechanisms of maturation and ageing of collagen. Mech. Ageing Dev. 1998;106(1–2):1–56. - PubMed
-
- Li Z.-R., Wang B., Chi C.-f., Zhang Q.-H., Gong Y.-d., Tang J.-J., Luo H.-y., Ding G.-f. Isolation and characterization of acid soluble collagens and pepsin soluble collagens from the skin and bone of Spanish mackerel (Scomberomorous Niphonius) Food Hydrocolloids. 2013;31(1):103–113.
-
- Lee C., Singla a., Lee a. Y. Biomedical applications of collagen. Int. J. Pharm. 2001;221(1–2):1–22. - PubMed
-
- Goulam Houssen Y., Gusachenko I., Schanne-Klein M.C., Allain A.J.M. Monitoring micrometer-scale collagen organization in rat-tail tendon upon mechanical strain using second harmonic microscopy. J. Biomech. 2011;44(11):2047–2052. - PubMed
LinkOut - more resources
Full Text Sources