Isolation and characterization of collagen from the cartilage of Amur sturgeon (Acipenser schrenckii) |
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| Affiliation: | 1. School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, PR China;2. Zhenjiang Kehua Aquaculture Development Company Limited, Zhenjiang 212134, PR China;1. Department of Traumatology and Hand Surgery, School of Medicine, University of Pécs, H-7624, Pécs, Szigeti Street 12, Hungary;2. Department of Pathology, School of Medicine, University of Pécs, H-7624, Pécs, Szigeti Street 12, Hungary;3. Department of Biophysics, School of Medicine, University of Pécs, H-7624, Pécs, Szigeti Street 12, Hungary;1. Department of Marine Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China;2. Shanghai Fisheries Research Institute, Shanghai 200433, China;1. State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China;2. Synergetic Innovation Center of Food Safety and Nutrition, Wuxi, Jiangsu Province 214122, China;3. Department of Food Science, Cornell University, Ithaca, NY 14853-7201, USA |
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| Abstract: | The collagen in Amur sturgeon cartilage was isolated using sodium chloride (salt-solubilized collagen, SSC, 2.18%), followed by acetic acid (acid-solubilized collagen, ASC, 27.04%) and then pepsin (pepsin-solubilized collagen, PSC, 55.92%). These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC (35.71 and 123.90 °C) were significantly higher than SSC (32.64 and 114.51 °C) and ASC (32.98 and 120.72 °C) assessed by circular dichroism and differential scanning calorimetry, which could be attributed to its high imino acid content (22.57%) and degree of hydroxylation (47.29%). Electrophoresis pattern showed that the SSC and ASC were type I collagen, while PSC was predominantly type II collagen along with other minor types. Infrared spectra confirmed their triple helical structure, and indicated more hydrogen bonding in ASC and more intermolecular crosslinks in PSC. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen. |
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| Keywords: | Collagen Cartilage Isolation Characterization |
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