Abstract
In search of alternative and safer sources of collagen for biomedical applications, the marine demosponges Axinella cannabina and Suberites carnosus, collected from the Aegean and the Ionian Seas, respectively, were comparatively studied for their insoluble collagen, intercellular collagen, and spongin-like collagen content. The isolated collagenous materials were morphologically, physicochemically, and biophysically characterized. Using scanning electron microscopy and transmission electron microscopy the fibrous morphology of the isolated collagens was confirmed, whereas the amino acid analysis, in conjunction with infrared spectroscopy studies, verified the characteristic for the collagen amino acid profile and its secondary structure. Furthermore, the isoelectric point and thermal behavior were determined by titration and differential scanning calorimetry, in combination with circular dichroism spectroscopic studies, respectively.
Highlights
Collagen is an ubiquitous high molecular weight fibrous protein occurring in both invertebrate and vertebrate organisms, existing in more than 20 different types depending on its role in distinct tissues [1,2]
The insoluble, intercellular, and spongin-like collagens were isolated from A. cannabina and S. carnosus, representing 12.6%, 3.0%, and 42.8% dry weight for the former and
As compared to that derived from terrestrial animals and other marine collagen sources, has been reported to differentiate in its characteristics, such as amino acid composition, which consecutively affects collagen’s thermal behavior, isoelectric pH, solubility, and many other properties
Summary
Collagen is an ubiquitous high molecular weight fibrous protein occurring in both invertebrate and vertebrate organisms, existing in more than 20 different types depending on its role in distinct tissues [1,2]. Its polypeptide chains are organized in a unique structure, in which three α-helices are intertwined forming a characteristic right-handed triple helix. These peptides are rich in glycine, proline, and hydroxyproline amino acids, all being crucial for the formation of the helical configuration [3]. Gelatin, the denatured form of collagen obtained by its partial hydrolysis, is used as an additive in the food processing industry and in nutraceuticals [6].
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