Extraction and characterization of highly purified collagen from bovine pericardium for potential bioengineering applications.

Autor: Santos MH; Department of Dentistry, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil; Center for Assessment and Development of Biomaterials-BioMat, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil. Electronic address: mariahelena.santos@gmail.com., Silva RM; Department of Dentistry, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil; Center for Assessment and Development of Biomaterials-BioMat, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil., Dumont VC; Department of Dentistry, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil; Center for Assessment and Development of Biomaterials-BioMat, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil., Neves JS; Center for Assessment and Development of Biomaterials-BioMat, Federal University of Vales do Jequitinhonha e Mucuri-UFVJM, Diamantina/MG 39100-000, Brazil., Mansur HS; Department of Metallurgical and Materials Engineering, Federal University of Minas Gerais-UFMG, Belo Horizonte/MG 31270-901, Brazil., Heneine LG; Department of Health Science, Ezequiel Dias Foundation-FUNED, Belo Horizonte/MG 30510-010, Brazil.
Jazyk: angličtina
Zdroj: Materials science & engineering. C, Materials for biological applications [Mater Sci Eng C Mater Biol Appl] 2013 Mar 01; Vol. 33 (2), pp. 790-800. Date of Electronic Publication: 2012 Nov 10.
DOI: 10.1016/j.msec.2012.11.003
Abstrakt: Bovine pericardium is widely used as a raw material in bioengineering as a source of collagen, a fundamental structural molecule. The physical, chemical, and biocompatibility characteristics of these natural fibers enable their broad use in several areas of the health sciences. For these applications, it is important to obtain collagen of the highest possible purity. The lack of a method to produce these pure biocompatible materials using simple and economically feasible techniques presents a major challenge to their production on an industrial scale. This study aimed to extract, purify, and characterize the type I collagen protein originating from bovine pericardium, considered to be an abundant tissue resource. The pericardium tissue was collected from male animals at slaughter age. Pieces of bovine pericardium were enzymatically digested, followed by a novel protocol developed for protein purification using ion-exchange chromatography. The material was extensively characterized by electrophoresis, scanning electron microscopy, energy dispersive X-ray spectroscopy, and infrared spectroscopy. The results showed a purified material with morphological properties and chemical functionalities compatible with type I collagen and similar to a highly purified commercial collagen. Thus, an innovative and relatively simple processing method was developed to extract and purify type I collagen from bovine tissue with potential applications as a biomaterial for regenerative tissue engineering.
(Copyright © 2012 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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