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中国精品科技期刊2020
吴长玲, 田甜, 王冬梅, 李波, 陈龙, 王中江, 李杨, 江连洲, 范志军. 低温超微粉碎对豆渣蛋白结构及功能性质的影响[J]. 食品工业科技, 2018, 39(23): 50-55. DOI: 10.13386/j.issn1002-0306.2018.23.009
引用本文: 吴长玲, 田甜, 王冬梅, 李波, 陈龙, 王中江, 李杨, 江连洲, 范志军. 低温超微粉碎对豆渣蛋白结构及功能性质的影响[J]. 食品工业科技, 2018, 39(23): 50-55. DOI: 10.13386/j.issn1002-0306.2018.23.009
WU Chang-ling, TIAN Tian, WANG Dong-mei, LI Bo, CHEN Long, WANG Zhong-jiang, LI Yang, JIANG Lian-zhou, FAN Zhi-jun. Effects of Superfine Comminution of Low Temperature on the Structural and Functional Properties of Soy Dregs Protein[J]. Science and Technology of Food Industry, 2018, 39(23): 50-55. DOI: 10.13386/j.issn1002-0306.2018.23.009
Citation: WU Chang-ling, TIAN Tian, WANG Dong-mei, LI Bo, CHEN Long, WANG Zhong-jiang, LI Yang, JIANG Lian-zhou, FAN Zhi-jun. Effects of Superfine Comminution of Low Temperature on the Structural and Functional Properties of Soy Dregs Protein[J]. Science and Technology of Food Industry, 2018, 39(23): 50-55. DOI: 10.13386/j.issn1002-0306.2018.23.009

低温超微粉碎对豆渣蛋白结构及功能性质的影响

Effects of Superfine Comminution of Low Temperature on the Structural and Functional Properties of Soy Dregs Protein

  • 摘要: 为研究低温超微粉碎对豆渣蛋白结构与功能性质的影响,明确低温超微粉碎对豆渣蛋白的作用机制。本文利用低温超微粉碎技术处理豆渣,采用荧光光谱法分析不同处理条件下豆渣蛋白的结构变化,并通过豆渣蛋白界面性质、溶解性、粒度分析及ζ-电位对其功能性质进行表征。结果表明:低温粉碎200目下豆渣蛋白性质最佳,其粒径分布稳定,体积平均粒径D4,3降低至(24.06±0.02)μm,ζ-电位绝对值增大至14.02±0.02;通过荧光光谱分析可知,低温超微粉碎使得豆渣蛋白结构发生解折叠,蛋白分子内疏水性氨基酸暴露。

     

    Abstract: To analyze the effects of superfine comminution of low temperature on the structure and functional properties of soy dregs protein and determin the mechanism of action of low temperature ultrafine pulverization on soy dregs protein. In this study,technology of superfine comminution of low temperature was used to process soy dregs. The structural changes of soy dregs under different treatment conditions were analyzed by fluorescence spectroscopy,and the functional properties of the soy dregs protein were characterized by the interface properties,solubility,particle size analysis and ζ-potentia. The results showed that the best soy dregs protein were obtained at 200 mesh under low temperature and particle size distribution was stable,D4,3 was significantly reduced to(24.06±0.02) μm,the absolute value of ζ-potential was significantly increased to 24.06±0.02. The fluorescence spectra showed that degrees by superfine comminution of low temperature induced the extension of soy dregs protein residued unfolds and the hydrophobic amino acids in the protein molecule exposed.

     

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