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中国精品科技期刊2020
郝俊杰, 马海乐, 罗敏, 郭晶晶, 李云亮. 聚能式脉冲逆流超声辅助热水提取鱼鳞胶原蛋白[J]. 食品工业科技, 2014, (11): 117-122. DOI: 10.13386/j.issn1002-0306.2014.11.017
引用本文: 郝俊杰, 马海乐, 罗敏, 郭晶晶, 李云亮. 聚能式脉冲逆流超声辅助热水提取鱼鳞胶原蛋白[J]. 食品工业科技, 2014, (11): 117-122. DOI: 10.13386/j.issn1002-0306.2014.11.017
HAO Jun-jie, MA Hai-le, LUO Min, GUO Jing-jing, LI Yun-liang. Energy-gathered pulsed ultrasonic-assisted hot water extraction of fish scale collagen[J]. Science and Technology of Food Industry, 2014, (11): 117-122. DOI: 10.13386/j.issn1002-0306.2014.11.017
Citation: HAO Jun-jie, MA Hai-le, LUO Min, GUO Jing-jing, LI Yun-liang. Energy-gathered pulsed ultrasonic-assisted hot water extraction of fish scale collagen[J]. Science and Technology of Food Industry, 2014, (11): 117-122. DOI: 10.13386/j.issn1002-0306.2014.11.017

聚能式脉冲逆流超声辅助热水提取鱼鳞胶原蛋白

Energy-gathered pulsed ultrasonic-assisted hot water extraction of fish scale collagen

  • 摘要: 本文旨在研究利用聚能式逆流脉冲超声波(28kHz/150W)强化鱼鳞胶原蛋白的提取。在单因素实验基础上,以提取率为指标,进行了响应面参数优化和数学模型回归的研究,同时检测了超声处理前后鱼鳞胶原蛋白傅立叶变换红外光谱的变化。研究表明,超声辅助热水提取鱼鳞胶原蛋白的最佳条件为:温度80℃、液料比40mL/g、提取时间60min、pH6、脉冲超声的发声时间8s与超声间歇时间5s,提取率为81.25%,与模型的预测值81.63%无显著差异;与传统热水提取法相比,超声辅助提取法的提取率增加了20.71%。胶原蛋白傅立叶变换红外光谱分析结果表明,超声处理后蛋白的酰胺Ⅰ和酰胺Ⅱ最大波峰发生了改变,说明超声处理前后胶原蛋白的二级结构发生了变化。 

     

    Abstract: In this work, an energy-gathered pulsed ultrasonic-assisted procedure of fish scale collagen extraction was investigated.Response surface methodology ( RSM) with a 3-factor, 3-lever Box-Behnken Design ( BBD) was conducted to ascertain the optimum ultrasound-assisted extraction parameters ( extraction temperature X1, ratio of solvent to solid X2, ultrasonic time X3) .The optimum conditions were determined to be extraction temperature 80℃, ratio of solid to solvent 40mL /g, extraction time 60min, pH6 and ultrasonic pulse mode 8s on and 5s off.Under this condition, the extraction efficiency of fish scale collagen could significantly increase from 67.31% to 81.25% and almost reached the model calculation value 81.63%.The FT-IR spectrum analysis revealed that ultrasonic-assisted treatment could cause the transfer of absorbance peak of acylamino residues I and II of fish scale collagen.

     

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