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Biology
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Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications
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Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications

A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Biotechnology".

Deadline for manuscript submissions: closed (31 August 2022) | Viewed by 28793

Special Issue Editor

Dr. Rafea Naffa

E-Mail Website
Guest Editor
New Zealand Leather & Shoe Research Association, Palmerston North, New Zealand
Interests: collagen; method development; enzymes; structural studies; skin; leather

Special Issue Information

Dear Colleagues,

Collagen is the most abundant structural proteins in animals and play an integral biological and structural role in the extracellular matrix. There are up to 28 different types of collagen in vertebrates, where most of them interact with other ECM proteins to form supramolecular network architecture which play a vital part in cell adhesion, migration and proliferation as well as providing strength. Although they all share a common feature of at least one triple helical domain, there are significant differences between the amino acid number and sequence, structure, and the role of different collagen types. The discovery of collagen structure by Crick et al. and Ramachandran et al. in 1955 has driven a rapid understanding of the molecular and structural properties of collagen. Such understanding guided further extraction and characterisation of collagen for different applications.

In the recent years, the beneficial effects of collagen and its peptides as functional food has attracted more scientific research interests, however understanding its composition and fibrillar structure and biological characteristics has proven crucial.

We you to submit your review and original research covering a broad range of topics in collagen and its applications. Area of particular interest but are not limited to:

  • Extraction of collagen from animal sources.
  • Characterisation of collagen.
  • Degradation of collagen.
  • Collagen peptides.
  • Collagen structure.
  • Types of collagen and their compositions.
  • Bio-analytical methods for collagen purification and characterisation.
  • Collagen applications.
  • Collagen as protein source in food.
  • Collagen in leather industry.
  • Novel Technology for collagen.
  • New trends in collagen.

Dr. Rafea Naffa
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biology is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • collagen
  • collagen peptides
  • mass spectrometry
  • extraction
  • composition

Published Papers (4 papers)

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Research

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22 pages, 4815 KiB  
Article
3D-Printed Hybrid Collagen/GelMA Hydrogels for Tissue Engineering Applications
by Anushree Nagaraj, Alaitz Etxabide Etxeberria, Rafea Naffa, Ghada Zidan and Ali Seyfoddin
Biology 2022, 11(11), 1561; https://doi.org/10.3390/biology11111561 - 25 Oct 2022
Cited by 12 | Viewed by 4087
Abstract
Bioprinting is an emerging technology involved in the fabrication of three-dimensional tissue constructs for the repair and regeneration of various tissues and organs. Collagen, a natural protein found abundantly in the extracellular matrix of several tissues, can be extracted from collagen-rich tissues of [...] Read more.
Bioprinting is an emerging technology involved in the fabrication of three-dimensional tissue constructs for the repair and regeneration of various tissues and organs. Collagen, a natural protein found abundantly in the extracellular matrix of several tissues, can be extracted from collagen-rich tissues of animals such as sheep, cows, rats, pigs, horses, birds, and marine animals. However, due to the poor printability of collagen bioinks, biocompatible collagen scaffolds that mimic the extracellular matrix (ECM) are difficult to fabricate using bioprinting techniques. Gelatin methacrylate (GelMA), a semi-synthetic polymer with tunable physical and chemical properties, has been found to be a promising biomaterial in various bioprinting applications. The printability of collagen can be improved by combining it with semi-synthetic polymers such as GelMA to develop hybrid hydrogels. Such hybrid hydrogels printed have also been identified to have enhanced mechanical properties. Hybrid GelMA meshes have not previously been prepared with collagen from ovine sources. This study provides a novel comparison between the properties of hybrid meshes with ovine skin and bovine hide collagen. GelMA (8% w/v) was integrated with three different concentrations (0.5%, 1%, and 2%) of bovine and ovine collagen forming hybrid hydrogels inks that were printed into meshes with enhanced properties. The maximum percentage of collagen suitable for integration with GelMA, forming hybrid hydrogels with a stable degradation rate was 1%. The water-soluble nature of ovine collagen promoted faster degradation of the hybrid meshes, although the structural crosslinking was identified to be higher than bovine hybrid meshes. The 1% bovine collagen hybrid meshes stood out in terms of their stable degradation rates. Full article
(This article belongs to the Special Issue Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications)
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12 pages, 285 KiB  
Article
Novel Assessment of Collagen and Its Crosslink Content in the Humerus from Primiparous Dairy Cows with Spontaneous Humeral Fractures Due to Osteoporosis from New Zealand
by Alvaro Wehrle-Martinez, Rafea Naffa, Penny Back, Chris W. Rogers, Kevin Lawrence, Trevor Loo, Andrew Sutherland-Smith and Keren Dittmer
Biology 2022, 11(10), 1387; https://doi.org/10.3390/biology11101387 - 23 Sep 2022
Cited by 5 | Viewed by 1640
Abstract
Numerous cases of spontaneous humeral fracture in primiparous dairy cows from New Zealand have prompted the study of the condition to establish probable causes or risk factors associated with the condition. Previous studies identified inadequate protein-calorie malnutrition as an important contributory factor. Earlier [...] Read more.
Numerous cases of spontaneous humeral fracture in primiparous dairy cows from New Zealand have prompted the study of the condition to establish probable causes or risk factors associated with the condition. Previous studies identified inadequate protein-calorie malnutrition as an important contributory factor. Earlier case studies also reported that ~50% of cows have low liver and/or serum copper concentration at the time of humeral fracture. Because copper is so closely associated with the formation of collagen cross-links, the aim of this study was to compare collagen and collagen crosslink content in the humerus from primiparous cows with and without humeral fractures and to determine the role of copper in the occurrence of these fractures. Humeri were collected from cows with and without humeral fractures, ground, and the collagen and collagen cross-link content measured using high-performance liquid chromatography. Collagen content was significantly higher in the humeri of cows without humeral fractures, while total collagen crosslink content was significantly higher in the humerus of cows with humeral fractures. These results indicate other factor/s (e.g., protein-calorie undernutrition) might be more important than the copper status in the occurrence of humeral fractures in dairy cows in New Zealand. Full article
(This article belongs to the Special Issue Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications)
11 pages, 2201 KiB  
Article
Structure and Strength of Bovine and Equine Amniotic Membrane
by Hannah C. Wells, Katie H. Sizeland, Nigel Kirby and Richard G. Haverkamp
Biology 2022, 11(8), 1096; https://doi.org/10.3390/biology11081096 - 23 Jul 2022
Cited by 1 | Viewed by 1881
Abstract
Thin, strong scaffold materials are needed for surgical applications. New materials are required, particularly those readily available, such as from non-human sources. Bovine amniotic membrane (antepartum) and equine amniotic membrane (postpartum) were characterized with tear and tensile tests. The structural arrangement of the [...] Read more.
Thin, strong scaffold materials are needed for surgical applications. New materials are required, particularly those readily available, such as from non-human sources. Bovine amniotic membrane (antepartum) and equine amniotic membrane (postpartum) were characterized with tear and tensile tests. The structural arrangement of the collagen fibrils was determined by small-angle X-ray scattering, scanning electron microscopy, and ultrasonic imaging. Bovine amnion had a thickness-normalized tear strength of 12.6 (3.8) N/mm, while equine amnion was 14.8 (5.3) N/mm. SAXS analysis of the collagen fibril arrangement yielded an orientation index of 0.587 (0.06) and 0.681 (0.05) for bovine and equine, respectively. This may indicate a relationship between more highly aligned collagen fibrils and greater strength, as seen in other materials. Amnion from bovine or equine sources are strong, thin, elastic materials, although weaker than other collagen tissue materials commonly used, that may find application in surgery as an alternative to material from human donors. Full article
(This article belongs to the Special Issue Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications)
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Review

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15 pages, 2106 KiB  
Review
Collagen Extraction from Animal Skin
by Andrea Marie E. Matinong, Yusuf Chisti, Kim L. Pickering and Richard G. Haverkamp
Biology 2022, 11(6), 905; https://doi.org/10.3390/biology11060905 - 13 Jun 2022
Cited by 45 | Viewed by 19838
Abstract
Collagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the [...] Read more.
Collagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the focus on literature published since 2000. The different pretreatment and extraction techniques that have been investigated for producing collagen from animal skins are reviewed. Pretreatment by enzymatic, acid or alkaline methods have been used. Extraction by chemical hydrolysis, salt solubilization, enzymatic hydrolysis, ultrasound assisted extraction and other methods are described. Post-extraction purification methods are also explained. This compilation will be useful for anyone wishing to use collagen as a resource and wanting to further improve the extraction and purification methods. Full article
(This article belongs to the Special Issue Collagen from Animal Biological Sources: Extraction, Purification, Characterisation and Applications)
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