title: 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.
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.
authors.affiliation: UR 370 QuaPA (Qualité de Produits Animaux) INRA, 63122 Saint-Genès-Champanelle, France; UR 1268 BIA (Biopolymères, Interactions, Assemblages) INRA, 44300 Nantes, France. Electronic address: vincenza.ferraro@inra.fr.
authors.forename: Vincenza
authors.initials: V
authors.lastname: Ferraro
authors.affiliation: UR 454 Microbiologie INRA, 63122 Saint-Genès-Champanelle, France.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Gaillard-Martinie
authors.affiliation: UR 370 QuaPA (Qualité de Produits Animaux) INRA, 63122 Saint-Genès-Champanelle, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Sayd
authors.affiliation: UR 370 QuaPA (Qualité de Produits Animaux) INRA, 63122 Saint-Genès-Champanelle, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Chambon
authors.affiliation: UR 1268 BIA (Biopolymères, Interactions, Assemblages) INRA, 44300 Nantes, France.
authors.forename: Marc
authors.initials: M
authors.lastname: Anton
authors.affiliation: UR 370 QuaPA (Qualité de Produits Animaux) INRA, 63122 Saint-Genès-Champanelle, France.
authors.forename: Véronique
authors.initials: V
authors.lastname: Santé-Lhoutellier
mesh_terms: D000375:Aging / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry* / Q000302:isolation & purification*; D003890:Desiccation / Q000379:methods*; D005269:Femur / Q000033:anatomy & histology* / Q000737:chemistry; D007700:Kinetics; D066329:Protein Aggregates; D020673:Protein Renaturation; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature; D013977:Tibia / Q000033:anatomy & histology* / Q000737:chemistry
chemical_list: D024042:Collagen Type I; D066329:Protein Aggregates
keywords: Bone; Collagen; Extraction; Protein; Self-assembly