Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-19T07:33:12.775Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of Glutaraldehyde on Properties of Membranes Prepared from Fish Scale Collagen

Published online by Cambridge University Press:  01 March 2012

Zhefeng Xu ,
Toshiyuki Ikoma ,
Tomohiko Yoshioka ,
Motohiro Tagaya ,
Satoshi Motozuka ,
Rena Matsumoto ,
Toshimasa Uemura  and
Junzo Tanaka
Zhefeng Xu
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN
Toshiyuki Ikoma
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN
Tomohiko Yoshioka
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN
Motohiro Tagaya
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN
Satoshi Motozuka
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN Department of Mechanical Engineering, Gifu National College of Technology, Kamimakuwa 2236-2, Motosu-si, Gifu 501-0495, JAPAN
Rena Matsumoto
Affiliation:
Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology, Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 3-5-8562, JAPAN
Toshimasa Uemura
Affiliation:
Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology, Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 3-5-8562, JAPAN
Junzo Tanaka
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute Technology University, O-okayama 2-12-1, Meguro-ku, Tokyo 152-8550 JAPAN
Get access

Abstract

Collagen fibril membranes (CFMs) with a high mechanical property were fabricated with a lateral face evaporation method, in which type I atelocollagen extracted from tilapia scales was used. The density and thickness of the CFM obtained were 0.51 ± 0.04 mg/cm3 and 50 ± 5 μm. The collagen fibrils in the CFM had a similar periodic stripped pattern of 67 nm with native collagen fibrils. The CFM was crosslinked in gaseous glutaraldehyde for different duration in order to increase the mechanical property. The crosslinking degrees of the CFMs analyzed by free amino groups gradually increased to 70.3 % against the exposure duration until 6 hours, and reached a plateau. The denaturation temperatures of the CFMs with the crosslinking degrees at 20.4 % to 43% were linearly increased from 49°C to 75°C. The tensile strength of the CFMs was slightly improved until the crosslinking degree at 33.3 % and then the tensile strength rapidly increased to be 68 MPa. It was suggested that a percolation phenomenon took place in the CFMs by crosslinking of collagen fibrils with polymerized GA molecules.

Keywords

biomaterialchemical synthesismicrostructure
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1418: Symposium LL/MM – Gels and Biomedical Materials , 2012 , mrsf11-1418-mm06-04
Copyright
Copyright © Materials Research Society 2012

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Boccafoschi, F., Habermehl, J., Vesentini, S., and Mantovani, D., Biomaterials 26, 7410–7417 (2005).10.1016/j.biomaterials.2005.05.052CrossRefGoogle Scholar
2. Lin, Y., Liu, D., Food Chemistry 99, 244–251 (2006).10.1016/j.foodchem.2005.06.053Google Scholar
3. Sylvie, R. B., Florence, R., Pathologie Biologie 53, 430–442 (2005).Google Scholar
4. Vernon, Robert B., Gooden, Michel D., Lara, Stephanie L., and Wight, Thomas N., Biomaterials 26, 3131–3140 (2005).CrossRefGoogle Scholar
5. Tai, B. C., Wan, A. C., and Ying, J. Y., Biomaterials 31, 5927–5935 (2010).CrossRefGoogle Scholar
6. Feng, Z. Q, Chu, X. H, Huang, N. P, Leach, M. K. et al. , Biomaterials 31, 3604–3612 (2010).Google Scholar
7. Dutta, R. C., Dutta, A. K., Biotechnology Advances 27, 334–339 (2009).10.1016/j.biotechadv.2009.02.002Google Scholar
8. Gómez-Guillén, M.C., Giménez, B., López-Caballero, M.E., and Montero, M.P., Food Hydrocolloids 25, 1813–1827 (2011).10.1016/j.foodhyd.2011.02.007Google Scholar
9. Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D., and Mann, S., International Journal of Biological Macromolecules 32, 199–204 (2003).10.1016/S0141-8130(03)00054-0Google Scholar
10. Takezawa, T., Fukuda, M., Mcintosh-Ambrose, W., Ko, J. A., Elisseeff, J., Haga, S., Ozaki, M., Kato, K., Wang, P. C., Uchino, T., and Nishida, T., Yakugaku Zasshi 130, 565–574 (2010).10.1248/yakushi.130.565Google Scholar
11. Jastrzebska, M., Wrzalik, R., Kocot, A., Zalewska-Rejdak, J. and Cwalina, B., J. Biomater. Sci. Polymer Edn 14, 185–197 (2003).CrossRefGoogle Scholar
12. Bigi, A., Cojazzi, G., Panzavolta, S., Roveri, N. and Rubini, K., Biomaterials 23, 4827–4832 (2002).10.1016/S0142-9612(02)00235-1CrossRefGoogle Scholar
13. Achet, D., He, X. W., Polymer 36,789–791 (1995).10.1016/0032-3861(95)93109-YGoogle Scholar
14. Kawahara, J., Ohmori, T., Ohkubo, T., Hattori, S., and Kawamura, M., Analy. Biochem. 201, 94–98 (1992)Google Scholar