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中国精品科技期刊2020
李秋雨,刘红梅,李彦,等. 鱼鳞胶原蛋白提取残渣中角蛋白的回收与表征[J]. 食品工业科技,2021,42(9):179−185. doi: 10.13386/j.issn1002-0306.2020070321.
引用本文: 李秋雨,刘红梅,李彦,等. 鱼鳞胶原蛋白提取残渣中角蛋白的回收与表征[J]. 食品工业科技,2021,42(9):179−185. doi: 10.13386/j.issn1002-0306.2020070321.
LI Qiuyu, LIU Hongmei, LI Yan, et al. Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue[J]. Science and Technology of Food Industry, 2021, 42(9): 179−185. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2020070321.
Citation: LI Qiuyu, LIU Hongmei, LI Yan, et al. Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue[J]. Science and Technology of Food Industry, 2021, 42(9): 179−185. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2020070321.

鱼鳞胶原蛋白提取残渣中角蛋白的回收与表征

Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue

  • 摘要: 为充分开发鱼鳞的经济价值,增加其回收利用率,本研究以草鱼鱼鳞为原料,研究了分离鱼鳞胶原蛋白的最佳方法以获得较纯的角蛋白,并以提取过胶原蛋白的鱼鳞残渣为原料,运用单因素实验和正交试验确定角蛋白的最优提取工艺,再对提取的鱼鳞角蛋白进行表征。结果表明:1%的柠檬酸溶液中加0.60 g胃蛋白酶于4 ℃下浸泡24 h,胶原蛋白去除率最高,去除效果及结构完整性最好;提取草鱼鱼鳞角蛋白的最优工艺条件为:提取温度60 ℃,氢氧化钠浓度9%,料液比1:12.5。鱼鳞角蛋白的紫外吸收峰分别在218.2、280.4 nm处,SDS-PAGE电泳显示鱼鳞角蛋白的表观分子量约为48 kDa,红外结果显示角蛋白的二级结构为α-螺旋,氨基酸组分的特征与羊毛角蛋白基本一致。

     

    Abstract: In order to fully develop the economic value of fish scales, expand the source of keratin, in this study, the collagen-extracted grass carp fish scale residues were used as raw materials, single factor experiment and orthogonal experiment were used to determine the optimal extraction process of keratin, and the extracted fish scale keratin was characterized. The results showed that under the condition of 60 g pepsin in 1% citric acid solution at 4 ℃ for 24 h, the highest collagen removal ratew as obtained, with the best removal effect and structural integrit. The optimal process conditions for extracting grass carp scale keratin were as follows: Extraction temperature 60 ℃, sodium hydroxide concentration 9%, material-liquid ratio 1:12.5. The UV absorption peaks of fish scale keratin were at 218.2, 280.4 nm, respectively. SDS-PAGE electrophoresis showed that the apparent molecular weight of fish scale keratin was about 48 kDa. Infrared results showed that the secondary structure of keratin was α-helix, and the characteristics of amino acid components were basically the same as wool keratin.

     

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