Collagen type I from bovine bone. Effect of animal age, bone anatomy and drying methodology on extraction yield, self-assembly, thermal behaviour and electrokinetic potential

Int J Biol Macromol. 2017 Apr:97:55-66. doi: 10.1016/j.ijbiomac.2016.12.068. Epub 2016 Dec 27.

Abstract

Natural collagen is easily available from animal tissues such as bones. Main limitations reported in the use of natural collagen are heterogeneity and loss of integrity during recovery. However, its natural complexity, functionality and bioactivity still remain to be achieved through synthetic and recombinant ways. Variability of physicochemical properties of collagen extracted from bovine bone by acetic acid was then investigated taking into account endogenous and exogenous factors. Endogenous: bovine's bones age (4 and 7 years) and anatomy (femur and tibia); exogenous: thermal treatments (spray-drying and lyophilisation). Scanning electron microscopy, spectroscopy (EDS, FTIR, UV/Vis and CD), differential scanning calorimetry (DSC), centesimal composition, mass spectrometry, amino acids and zeta-potential analysis were used for the purpose. Age correlated negatively with yield of recovery and positively with minerals and proteoglycans content. Comparing the anatomy, higher yields were found for tibias, and higher stability of tibias collagen in solution was noticed. Whatever the age and the anatomy, collagens were able to renature and to self-assemble into tri-dimensional structures. Nonetheless thermal stability and kinetics of renaturation were different. Variability of natural collagen with bone age and anatomy, and drying methodology, may be a crucial advantage to conceive tailor-made applications in either the biological or technical sector.

Keywords: Bone; Collagen; Extraction; Protein; Self-assembly.

MeSH terms

  • Aging / metabolism*
  • Animals
  • Cattle
  • Collagen Type I / chemistry*
  • Collagen Type I / isolation & purification*
  • Desiccation / methods*
  • Femur / anatomy & histology*
  • Femur / chemistry
  • Kinetics
  • Protein Aggregates
  • Protein Renaturation
  • Protein Stability
  • Protein Structure, Secondary
  • Temperature*
  • Tibia / anatomy & histology*
  • Tibia / chemistry

Substances

  • Collagen Type I
  • Protein Aggregates