文章摘要
引用本文:
海蜇胶原蛋白的制备及理化性质研究
The preparation, the physical and chemical properties of the jellyfish collagen
投稿时间:2017-01-22  修订日期:2017-05-10
DOI:
中文关键词: 海蜇  非变性  胶原蛋白  中低温  理化性质
英文关键词: jellyfish  non-degenerated  collagen  medium and low temperature  physical and chemical properties
基金项目:福建省海洋高新产业发展专项资助(闽海洋高新[2016] 04号)
作者单位E-mail
李玉芬 福州大学生物科学与工程学院 1452716838@qq.com 
郑明星 福州大学生物科学与工程学院  
朱 凡 福州大学生物科学与工程学院  
林娟 福州大学生物科学与工程学院 ljuan@fzu.edu.cn 
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中文摘要:
      以海蜇加工下脚料为原料,建立在中低温条件下以柠檬酸为提取剂的胶原蛋白制备工艺,并对海蜇胶原蛋白的理化性质进行分析。结果表明,海蜇加工下脚料中干基组分占7.00%,其中胶原蛋白占干基总量的44.91%;海蜇胶原蛋白的最佳酶法提取工艺条件为:提取温度15℃、柠檬酸浓度0.05 mol/L、胃蛋白酶添加量1.5%(g/g)、料液比1:2.0(g/mL)和提取时间8 h,在该条件下胶原蛋白提取率为97.41%。十二烷基硫酸钠聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate polyacrylamide gel electrophoresis ,SDS-PAGE) 表明其可能结构为[α1]3,单链分子量约124 kDa;氨基酸分析显示,其甘氨酸(glycine ,Gly)含量最高,占总氨基酸的25.16%,脯氨酸(proline ,Pro)和羟脯氨酸(hydroxyproline, Hyp)的含量分别为7.62%和9.32%,未检测到半胱氨酸(cysteine ,Cys) 和酪氨酸(tyrosine ,Tyr);傅立叶红外光谱分析表明,其保留了完整的三螺旋结构;黏度及溶解性特征显示,其等电点pI值在6-9之间,在≤1和≥10的pH值范围内结构趋于不稳定,热变性温度为22.7℃,在大于1.0 mol/L的NaCl溶液中基本析出。
英文摘要:
      To analyze the physical and chemical properties of jellyfish collagen, the leftover jellyfish was used as raw material, and treated with preparation technology. The preparation technology for collagen was based on the low-temperature condition and citric acid which worked as an extraction agent. The optimum enzymatic extraction condition was: 15 ℃, 0.05 mol/L citric acid concentration, 1.5% (m/m) pepsin addition, 1:2 (m/v) solid-liquid ratio and 8 h extraction time. The results showed that jellyfish processing scraps were 7.00 % of the dry base component, and collagen accounted 44.91% of the total dry basis, collagen extraction yield of 97.41%. By performing purified collagen on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the result demonstrated that collagen as Type I marine collagen in which three α1 chains each other. Moreover, the predicted mass for a α1 structure is 124 kDa. In amino acids composition analysis, glycine (Gly) occupied the highest percentage 25.16% in the collagen extracted. The percentage of Proline (Pro) and Hydroxyproline (Hyp) were respectively 7.62% and 9.32%. Whereas, Cysteine (Cys) and Tyrosine (Tyr) were not detected. Fourier Transform Infrared Spectroscopy (FTIR) data of the collagen revealed that stable triple-helical structure was existence. Meanwhile, the viscosity and solubility of purified collagen were measured to evaluate the pI value of collagen (about 6-9) and thermal denaturation temperature (22.7℃). According to the experimental results, collagen would precipitate completely in NaCl solution when its concentration was above 1.0 mol/L.
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