SPI挂面特性与其蛋白质结构特征的相关性  

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

作　　者：冯蕾[1] 李梦琴[1] 李超然[1] 

机构地区：[1]河南农业大学食品科学技术学院,河南郑州450002

出　　处：《现代食品科技》2014年第1期55-62,共8页Modern Food Science and Technology

基　　金：河南省教育厅自然科学研究计划项目(2010A550008)

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（10．53～14．22gmol／L），二歪《键含量整体波动降低（12．26-6．56gmol／L）；酰胺I谱带（1700cm-1～1600cm-1）中蛋白质二级结构经过去卷积，二阶导数拟合，出现p．折叠片层，延伸及分子内耦合，β-撕叠、叶螺旋、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-撕叠结构含量呈极显著正相关，与a-螺旋、β转角以及反向平行结构含量呈极显著负相关。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 pmol/L） and disulfide bond content decreased in volatility （12.26-5.56 pmol/L）. Meanwhile, the characteristic peaks in the secondary structures of protein, including anti-parallel -sheet, aggregated strands, β-strand, a-helix, 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 strucatres of anti-parallel β-sheet, aggregated strands, and strand were highly significant positive correlation. The percentage of characteristic peak in protein secondary structure including a-helix, β-sheet, reverse parallel structure was negative correlation.

关 键 词：挂面特性 大豆分离蛋白质 蛋白质二级结构 相关性 

分 类 号：TS213.24[轻工技术与工程—粮食、油脂及植物蛋白工程]