Effect of Heat Level and Expose Time on Denaturation of Collagen Tissues

Derman I. D. , Senel E. C. , Ferhanoğlu O., Çilesiz F. İ. , KAZANCI M.

CELLULAR AND MOLECULAR BIOENGINEERING, 2020 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume:
  • Publication Date: 2020
  • Doi Number: 10.1007/s12195-020-00653-w
  • Journal Indexes: Science Citation Index Expanded, Scopus, Academic Search Premier, Aerospace Database, Agricultural & Environmental Science Database, BIOSIS, Communication Abstracts, EMBASE, INSPEC, Metadex, Civil Engineering Abstracts


Introduction The applied heat level and expose time are main issues in certain operations/applications, such as a laser assisted tissue welding, preparation of collagen-based biomaterials (films, implants). Therefore, the precise investigation of these parameters is crucial. The results can serve as a guideline to assess potential effects while maintaining the functionality of the collagen structures. Methods Collagen tissues from rat-tail tendon, calfskin, and bones are soaked in buffer solutions, then examined by microscope at different temperature levels. Results Increase in temperature reduced the microscopically observed collagen crimp contrast for calfskin and rat-tail tendons but not for bone tissues. The contrast level for rat tail tendon decreased down to 80% of its initial value at 37, 157, and 266 s for 70, 65, and 60 degrees C, respectively. The decrease in the crimp contrast was about only 25% and 2% at 55 and 50 degrees C after 2 h, respectively. 50% drop in contrast level was occurred for the skin samples at 16, 90, 110 and 1900 s for 70, 65, and 60 degrees C, respectively. The bone samples, did not show any significant differences in contrast levels. Conclusion The observed denaturation behaviours are in line with Arrhenius Law. This study could be expanded on to other types of tissues at wider temperature ranges to make a guideline for biological/medical processes that radiate heat in order to assess their side effects on collagen and other proteins.