Extraction and characterization of highly purified collagen from bovine pericardium for potential bioengineering applications
Creators
- 1. Center for Assessment and Development of Biomaterials—BioMat, Federal University of Vales do Jequitinhonha e Mucuri—UFVJM, Diamantina/MG 39100–000 (Brazil)
- 2. Department of Dentistry, Federal University of Vales do Jequitinhonha e Mucuri—UFVJM, Diamantina/MG 39100–000 (Brazil)
- 3. Department of Metallurgical and Materials Engineering, Federal University of Minas Gerais—UFMG, Belo Horizonte/MG 31270–901 (Brazil)
- 4. Department of Health Science, Ezequiel Dias Foundation—FUNED, Belo Horizonte/MG 30510–010 (Brazil)
Description
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. - Highlights: ► Type I collagen was obtained from bovine pericardium, an abundant tissue resource. ► A simple and feasible processing technique was developed to purify bovine collagen. ► The appropriate process may be performed on industrial scale. ► The pure collagen presented appropriate morphological and molecular characteristics. ► The purify collagen has shown potential use as a biomaterial in tissue engineering.
Availability note (English)
Available from http://dx.doi.org/10.1016/j.msec.2012.11.003Additional details
Identifiers
- DOI
- 10.1016/j.msec.2012.11.003;
- PII
- S0928-4931(12)00520-6;
Publishing Information
- Journal Title
- Materials Science and Engineering. C, Biomimetic Materials, Sensors and Systems
- Journal Volume
- 33
- Journal Issue
- 2
- Journal Page Range
- p. 790-800
- ISSN
- 0928-4931
INIS
- Country of Publication
- Netherlands
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 44116386
- Subject category
- S36: MATERIALS SCIENCE;
- Descriptors DEI
- ABSORPTION SPECTROSCOPY; CATTLE; COLLAGEN; EXTRACTION; IMPURITIES; INFRARED SPECTRA; ION EXCHANGE CHROMATOGRAPHY; PERICARDIUM; POTENTIALS; SCANNING ELECTRON MICROSCOPY; X-RAY SPECTROSCOPY
- Descriptors DEC
- ANIMALS; BODY; CARDIOVASCULAR SYSTEM; CHROMATOGRAPHY; DOMESTIC ANIMALS; ELECTRON MICROSCOPY; HEART; MAMMALS; MEMBRANES; MICROSCOPY; ORGANIC COMPOUNDS; ORGANS; PROTEINS; RUMINANTS; SCLEROPROTEINS; SEPARATION PROCESSES; SEROUS MEMBRANES; SPECTRA; SPECTROSCOPY; VERTEBRATES
Optional Information
- Copyright
- Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.