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SPI挂面特性与其蛋白质结构特征的相关性
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作者简介:冯蕾(1987-),女,硕士,研究方向为食品科学 通讯作者:李梦琴(1965-),女,副教授,研究方向为食品科学与农产品加工

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河南省教育厅自然科学研究计划项目(2010A550008)


The Correlation of Protein Structural Features and Properties of Dry Noodles Added with SPI
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    摘要:

    采用质构分析、核磁共振及傅里叶红外光谱技术研究了不同添加量SPI对挂面的烹调性质、质地特性、水分状态及蛋白质结构特征参数的影响,结果表明:大豆分离蛋白显著影响挂面的烹调性质以及质地性质;添加大豆分离蛋白的挂面的T21增加,T22减小;随大豆分离蛋白含量的增加,挂面中巯基含量波动上升(10.53~14.22 μmol/L),二硫键含量整体波动降低(12.26~6.56 μmol/L);酰胺I谱带(1700 cm-1~1600 cm-1)中蛋白质二级结构经过去卷积,二阶导数拟合,出现β-折叠片层,延伸及分子内耦合,β-折叠、α-螺旋、β-转角、β-折叠片层、反向平行五个特征峰,且随着SPI添加量增加,蛋白质二级结构的百分含量变化差异显著;SPI挂面的弯曲距离与蛋白质二级结构中β-折叠片层,延伸及分子内耦合和β-折叠结构含量呈极显著正相关,与α-螺旋、β转角以及反向平行结构含量呈极显著负相关。

    Abstract:

    The properties and protein structural features of dry noodles added with soybean protein isolate (SPI) were analyzed by texture analysis,NMR and FT-IR technologies. The results showed that SPI had significant influence on texture and cooking properties of dry noodles. T21 of dry noodle added with SPI was increased while T22 was decreased. When addition level of SPI was increased, hydrosulphonyl content of dry noodle fluctuated increased (10.53~14.22 μmol/L) and disulfide bond content decreased in volatility (12.26~6.56 μmol/L). Meanwhile, the characteristic peaks in the secondary structures of protein, including anti-parallel β-sheet, aggregated strands, β-strand, α-helix, β-sheet, extension and intramolecular coupling were appeared. With SPI content increased, the percentage of protein secondary structures displayed significant difference. The bending distance to dry noodle and percentage of characteristic peak in protein secondary structures of anti-parallel β-sheet, aggregated strands, and β-strand were highly significant positive correlation. The percentage of characteristic peak in protein secondary structure including α-helix, β-sheet, reverse parallel structure was negative correlation.

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冯蕾,李梦琴,李超然. SPI挂面特性与其蛋白质结构特征的相关性[J].现代食品科技,2014,30(1):55-62.

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  • 收稿日期:2013-09-04
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  • 在线发布日期: 2014-02-18
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