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Review
. 2014 Dec 5;12(12):5881-901.
doi: 10.3390/md12125881.

Marine origin collagens and its potential applications

Affiliations
Review

Marine origin collagens and its potential applications

Tiago H Silva et al. Mar Drugs. .

Abstract

Collagens are the most abundant high molecular weight proteins in both invertebrate and vertebrate organisms, including mammals, and possess mainly a structural role, existing different types according with their specific organization in distinct tissues. From this, they have been elected as one of the key biological materials in tissue regeneration approaches. Also, industry is constantly searching for new natural sources of collagen and upgraded methodologies for their production. The most common sources are from bovine and porcine origin, but other ways are making their route, such as recombinant production, but also extraction from marine organisms like fish. Different organisms have been proposed and explored for collagen extraction, allowing the sustainable production of different types of collagens, with properties depending on the kind of organism (and their natural environment) and extraction methodology. Such variety of collagen properties has been further investigated in different ways to render a wide range of applications. The present review aims to shed some light on the contribution of marine collagens for the scientific and technological development of this sector, stressing the opportunities and challenges that they are and most probably will be facing to assume a role as an alternative source for industrial exploitation.

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Figures

Figure 1
Figure 1
Increment on the number of papers on collagen, marine collagen and in total, published in the last 13 years (XXI century), taking 2001 as reference. The data was collected from search in ISI Web of Knowledge™ using the terms collagen and marine collagen.
Figure 2
Figure 2
SDS-PAGE pattern of collagen extracted from the skin of codfish Gadus morhua by acetic acid treatment (ASC) and in the presence of pepsin (PSC).
Figure 3
Figure 3
DSC thermogram of ASC and PSC extracted from the skin of codfish, obtained at a scan rate of 1 °C·min−1.
Figure 4
Figure 4
FTIR spectra of ASC and PSC extracted from skin of codfish, indicating the amide characteristic bands of collagen.

References

    1. Vanderrest M., Garrone R. Collagen family of proteins. FASEB J. 1991;5:2814–2823. - PubMed
    1. Gelse K., Poschl E., Aigner T. Collagens—Structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 2003;55:1531–1546. doi: 10.1016/j.addr.2003.08.002. - DOI - PubMed
    1. Prockop D.J., Kivirikko K.I. Collagens—Molecular-biology, diseases, and potentials for therapy. Ann. Rev. Biochem. 1995;64:403–434. doi: 10.1146/annurev.bi.64.070195.002155. - DOI - PubMed
    1. Ferreira A.M., Gentile P., Chiono V., Ciardelli G. Collagen for bone tissue regeneration. Acta Biomater. 2012;8:3191–3200. doi: 10.1016/j.actbio.2012.06.014. - DOI - PubMed
    1. Deyl Z., Miksik I., Eckhardt A. Preparative procedures and purity assessment of collagen proteins. J. Chromatogr. B. 2003;790:245–275. doi: 10.1016/S1570-0232(03)00158-2. - DOI - PubMed

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