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. 2014 Jun 27;12(7):3852-73.
doi: 10.3390/md12073852.

Type II collagen and gelatin from silvertip shark (Carcharhinus albimarginatus) cartilage: isolation, purification, physicochemical and antioxidant properties

Elango Jeevithan  1 , Bin Bao  2 , Yongshi Bu  3 , Yu Zhou  4 , Qingbo Zhao  5 , Wenhui Wu  6
Affiliations

Type II collagen and gelatin from silvertip shark (Carcharhinus albimarginatus) cartilage: isolation, purification, physicochemical and antioxidant properties

Elango Jeevithan et al. Mar Drugs. .

Abstract

Type II acid soluble collagen (CIIA), pepsin soluble collagen (CIIP) and type II gelatin (GII) were isolated from silvertip shark (Carcharhinus albimarginatus) cartilage and examined for their physicochemical and antioxidant properties. GII had a higher hydroxyproline content (173 mg/g) than the collagens and cartilage. CIIA, CIIP and GII were composed of two identical α1 and β chains and were characterized as type II. Amino acid analysis of CIIA, CIIP and GII indicated imino acid contents of 150, 156 and 153 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CIIA, CIIP and GII were observed, which suggested that the isolation process affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of GII (32.5 °C) was higher than that of CIIA and CIIP. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIP was greater than that of CIIA and GII. SEM microstructure of the collagens depicted a porous, fibrillary and multi-layered structure. Accordingly, the physicochemical and antioxidant properties of type II collagens (CIIA, CIIP) and GII isolated from shark cartilage were found to be suitable for biomedical applications.

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Figures

Figure 1
Figure 1
(a) Electrophoretic pattern of type II collagens and type II gelatin isolated form shark cartilage; (b) Purification of type II collagen and type II gelatin by gel filtration chromatography. The horizontal lines in the chromatograms represent pooled fractions that were analyzed by SDS-PAGE. GII: type II gelatin, CIIA: type II acid soluble collagen, CIIP: type II pepsin soluble collagen.
Figure 2
Figure 2
Peptide map of collagen and gelatin isolated form shark cartilage. CIIP: type II pepsin soluble collagen, CIIA: type II acid soluble collagen, GII: type II gelatin, M: Marker.
Figure 3
Figure 3
Relative viscosity of type II collagens and type II gelatin. The viscosity obtained at 5 °C was considered as 100%. CIIP: type II pepsin soluble collagen, CIIA: type II acid soluble collagen, GII: type II gelatin.
Figure 4
Figure 4
Effect of pH (A) and salt concentration (B) on the solubility of collagens and gelatin. The highest solubility of collagens and gelatin was considered as 100% solubility. CIIP: type II pepsin soluble collagen, CIIA: type II acid soluble collagen, GII: type II gelatin.
Figure 5
Figure 5
DSC thermograms of type II collagens and type II gelatin. CIIP: type II pepsin soluble collagen, CIIA: type II acid soluble collagen, GII: type II gelatin.
Figure 6
Figure 6
FTIR spectra of type II collagens and type II gelatin. CIIP: type II pepsin soluble collagen, CIIA: type II acid soluble collagen, GII: type II gelatin.
Figure 7
Figure 7
Circular dichroism spectra of type II collagens and type II gelatin. formula image type II pepsin soluble collagen; formula image type II acid soluble collagen; formula image GII-type II gelatin.
Figure 8
Figure 8
Scanning electron microscopic structure of type II collagens and type II gelatin isolated from silvertip shark cartilage. A1, A2, A3: type II pepsin soluble collagen; B1, B2, B3: type II acid soluble collagen; C1, C2, C3: type II gelatin.
See this image and copyright information in PMC

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