重水环境下的氧化大豆蛋白傅里叶变换红外(FT-IR)分析  

FT-IR Spectroscopy Analysis of Oxidative Soybean Proteins in D_2O

作　　者：黄友如[1] 华欲飞[2] 张根华[1] 费薇[1] 闵娴[1] 

机构地区：[1]常熟理工学院生物与食品工程学院,常熟215500 [2]江南大学食品学院,无锡214036

出　　处：《中国粮油学报》2010年第5期19-23,29,共6页Journal of the Chinese Cereals and Oils Association

基　　金：国家自然科学基金(20476040)

摘　　要：应用傅里叶变换红外研究了不同亚油酸浓度下脂肪氧合酶催化诱导产生的大豆蛋白聚集体的结构变化。结果表明,由LOX催化LA氧化诱导的大豆蛋白质聚集,反映在红外光谱中,具有两个较为明显的特征,一是1 610 cm-1（RSP4和RSP5）或1 615 cm-1（RSP2和RSP3）附近谱峰分量的出现,二是酰胺I′各谱峰分量向低波数方向位移。此结论是在对反应体系中LA浓度在3.14×10-3~7.51×10-3mol/L范围之间的反应样品研究后得出的,说明反应体系中LA浓度不同,蛋白质分子间相互作用的强度不同;由于分子间β-折叠的形成与蛋白质分子间较强的相互作用有关,这些特征谱峰的出现反映了因氧化性修饰而发生聚集的蛋白质分子之间氢键作用的加强。The molecular structure of soybean protein aggregates formed at different linoleic acid concentration catalyzed by lipoxygenase were examined by FT-IR.Results： The linoleic acid-induced aggregation of soybean proteins is characterized by the appearance of a component located near 1 610 cm-1 in samples RSP4 and RSP5,or near 1 615 cm-1 in samples RSP2 and RSP3,and by another fact that all of the amide I′ components shift to lower wave numbers in the samples.This observation is made at the linoleic acid concentrations between 3.14×10-3 and 7.51×10-3 mol/L,suggesting that the intensity of the intermolecular interactions are different in the samples.Since the formation of intermolecular β-sheets seems to be involved in stronger interactions between proteins,the appearance of the characteristic components is a result of strengthening of H-bonds between aggregated proteins modified by linoleic acid oxidation.

关 键 词：大豆蛋白 脂肪氧合酶 亚油酸 氧化性修饰 FT-IR 

分 类 号：TS201.21[轻工技术与工程—食品科学] TQ645.99[轻工技术与工程—食品科学与工程]