基于红外光谱分析河套春小麦储藏期蛋白质二级结构变化  

Changes in secondary structure of Hetao spring wheat protein under storage analyzed by fourier transform infrared spectroscopy

作　　者：苏靖 石晶红[1] 王金帅 雍雅萍[1] SU Jing;SHI Jing-hong;WANG Jin-shuai;YONG Ya-ping(Hetao College,Bayan Nur 015000,Inner Mongolia,China;Inner Mongolia Hengfeng Food Industry(Group)Co.,Ltd,Bayan Nur 015000,Inner Mongolia,China)

机构地区：[1]河套学院,内蒙古巴彦淖尔015000 [2]内蒙古恒丰食品工业(集团)股份有限公司,内蒙古巴彦淖尔015000

出　　处：《粮食与油脂》2021年第11期24-27,35,共5页Cereals & Oils

基　　金：河套学院自然科学青年项目(HYZQ201717)。

摘　　要：以储藏前小麦为对照,采用傅里叶变换红外光谱法研究储藏温度、时间对小麦中蛋白质二级结构的影响。结果表明,储藏期内小麦蛋白的酰胺I带均向低波数方向发生不同程度的红移,表明疏水氨基酸残基暴露形成分子间氢键,二级结构发生变化。其中,α-螺旋和总β-折叠含量显著减少(P<0.05),β-转角含量显著增加(P<0.05),储藏后期出现无规则卷曲(P<0.05)。河套春小麦蛋白二级结构随着储藏时间的增加,由有序转化为无序。相对低温条件下储藏可以延缓这些转化,有利于小麦品质的保持。Fourier transform infrared spectroscopy(FT-IR)was used to study the effect of storage time and temperature on the secondary structure of wheat proteins.The results showed that different storage time could result in different degrees of red shift of wheat protein amideⅠbands to lower wave numbers,suggesting that intermolecular hydrogen bonds were formed between exposed hydrophobic amino acid residues and the secondary structure composition of wheat proteins changed significantly.Both a-helix content and the totalβ-sheet content decreased significantly(P<0.05),β-turn content increased significantly(P<0.05),and random coil content appeared in the late storage(P<0.05).Overall,the secondary structure of hetao spring wheat protein changed from order to disorder with the increase of storage time.Compared with different storage conditions,there were fewer transformations in wheat which was stored at the low temperature,and under this storage condition,wheat had better quality.

关 键 词：傅里叶变换红外光谱 蛋白质二级结构 储藏 春小麦 

分 类 号：TS210.1[轻工技术与工程—粮食、油脂及植物蛋白工程]