| 水母胶原蛋白的提取及性能研究 |
| 投稿时间：2020-08-19 修订日期：2020-10-16 点此下载全文 |
| 引用本文：仇雷雷,王博,邹帅军,王倩倩,张黎明.水母胶原蛋白的提取及性能研究[J].药学实践杂志,2020,38(6):509~515 |
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| 基金项目:国家自然科学基金项目(81974496) |
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| 中文摘要:目的 优化越前水母(Nemopilema nomurai)胶原蛋白提取工艺，并探究其性能。方法 利用乙酸和胃蛋白酶提取胶原蛋白，通过盐析和超滤纯化水母胶原蛋白粗提物，并对水母胶原蛋白进行表征和性能分析。结果 水母胶原蛋白纯度97%，得率33%（干重）；X射线衍射、紫外光谱和傅里叶变换红外光谱检测结果表明，水母胶原蛋白在提取和纯化过程中保持了胶原蛋白三螺旋结构；氨基酸组成和凝胶电泳分析提示，水母胶原蛋白符合Ⅰ型胶原蛋白特征。溶解度实验表明，水母胶原蛋白在pH 3～5，NaCl浓度小于0.9 mol/L的条件下都具有良好的溶解性。结论 所得水母胶原蛋白与牛Ⅰ型胶原蛋白特征相似，有望成为新的胶原蛋白资源。 |
| 中文关键词:越前水母 水母 胶原蛋白 提取 纯化 |
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| Isolation and characterization of collagen from the jellyfish Nemopilema nomurai |
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| Abstract:Objective To optimize the extraction process of collagen from the jellyfish (Nemopilema nomurai) and explore its characters.Methods The collagen was extracted with acetic acid and pepsin from jellyfish. The crude jellyfish collagen was purified by salting out and ultrafiltration. The purified collagen was characterized and analyzed by XRD (X-ray diffraction), UV (ultraviolet spectroscopy) and FTIR (fourier transform infrared spectroscopy).Results The purity of jellyfish collagen was 97%, the yield was 33% (dry weight). The jellyfish collagen maintained its triple helix structure during the extraction and purification process. Jellyfish collagen conformed to the characteristics of type I collagen according to amino acid composition and gel electrophoresis analysis. The jellyfish collagen exhibited a good solubility under the conditions of pH 3–5 and less than 0.9 mol/L of NaCl.Conclusion The extracted jellyfish collagen exhibited similar characteristics with bovine type I collagen and was a potential new source of collagen. |
| keywords:Nemopilema nomurai jellyfish collagen extraction purification |
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