Physicochemical Properties of Pepsin-Solubilized Collagen Extracted from Nile Tilapia (Oreochromis niloticus) Scale |
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| Authors: | Shaokui Zeng Juanjuan Yin Zhihong Jiang Wenlong Wu Xudong Zhao |
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| Institution: | 1. Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang, P.R. China;2. Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, Zhanjiang, P.R. China;3. College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, P.R. China;4. Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, Zhanjiang, P.R. China |
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| Abstract: | ABSTRACTThe aim was to investigate the physicochemical properties of pepsin-solubilized collagen (PSC) extracted from fish scales of Nile tilapia. The results indicated that Nile tilapia scales are rich in collagen. Therefore, the scales are a promising cost-effective collagen source. The conversion of hydroxyproline to collagen was 12.9. Based on the patterns of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), PSC comprised at least two different α chains, α1 and α2, and was classified to be type I with no disulfide. Fourier transform infrared spectroscopy spectrum showed that the bands of amide A, I, and II of PSC were found at 3,301, 1,631, and 1,239 cm?1 wavelength. The content of imino acids was 187 residues per 1,000 total amino acid residues. Maximum solubility was observed at pH 4, and minimum was at pH 7. Almost no change in solubility was observed in the presence of NaCl up to 2% (w/v), and the decrease was more pronounced with increasing NaCl concentration. The temperature of denaturation was 35.4°C. Results show that PSC has physicochemical properties that can be applied in the cosmetics, biomedical, pharmaceutical, and food industries. |
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| Keywords: | Tilapia pepsin-solubilized collagen amino acids denaturation temperature |
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