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中国精品科技期刊2020
樊雪静, 刘红玉, 迟玉杰. 加热对大豆分离蛋白寡糖复合溶液性质的影响[J]. 食品工业科技, 2017, (17): 38-44. DOI: 10.13386/j.issn1002-0306.2017.17.008
引用本文: 樊雪静, 刘红玉, 迟玉杰. 加热对大豆分离蛋白寡糖复合溶液性质的影响[J]. 食品工业科技, 2017, (17): 38-44. DOI: 10.13386/j.issn1002-0306.2017.17.008
FAN Xue-jing, LIU Hong-yu, CHI Yu-jie. Effect of heating on the properties of composite solution of soybean protein isolated-oligosaccharides[J]. Science and Technology of Food Industry, 2017, (17): 38-44. DOI: 10.13386/j.issn1002-0306.2017.17.008
Citation: FAN Xue-jing, LIU Hong-yu, CHI Yu-jie. Effect of heating on the properties of composite solution of soybean protein isolated-oligosaccharides[J]. Science and Technology of Food Industry, 2017, (17): 38-44. DOI: 10.13386/j.issn1002-0306.2017.17.008

加热对大豆分离蛋白寡糖复合溶液性质的影响

Effect of heating on the properties of composite solution of soybean protein isolated-oligosaccharides

  • 摘要: 本文以大豆分离蛋白(SPI)与寡糖(棉子糖与水苏糖)为原料,考察了加热(60,65,70,75,80、85℃)对SPI与寡糖聚合机理以及复合物乳化特性的影响。主要探讨了形成复合物的主要作用力、复合物特征、结构特性与功能特性的关系。研究发现,加热使复合溶液整体的Zeta电位升高,浊度增加,粒度分布右移,说明SPI与寡糖在加热条件下通过静电作用形成可溶性复合物,荧光强度降低从结构角度证实了蛋白质与寡糖的静电相互作用,同时,复合物的功能性质较SPI有所改善,SPI-水苏糖与SPI-棉子糖复合溶液乳化性和起泡性在75℃时达到最大,乳化性分别提高了32.7%和19.9%。 

     

    Abstract: In this paper, soybean protein isolated and oligosaccharides ( raffinose and stachyose) were used as raw materials, the influence of heating ( 65, 70, 75, 80, 85 ℃) on the emulsifying properties of compound and polymerization mechanism were investigated.The relationships among the major acting force producing the compound, characters of compounds, their structure features and functional traits were discussed. The research found that heating would raise the Zeta electric potential of the solution, intensify the turbidity and shift the distribution of granularity towards the right direction which illustrated that SPI and oligosaccharides would form soluble compound when heated. Moreover the decrease of fluorescence intensity verified the static interaction of protein and oligosaccharides in structural aspect.Simultaneously, the function of compounds was ameliorated more than that of proteins. The emulsification and foamability of SPI-raffinose and SPI-lupeose achieve their maximal value in75 ℃, which was increased by 32.7% and 19.9%.

     

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