储藏微环境对小麦蛋白质二级结构影响  

Influence of storage microenvironment to the secondary structure in wheat proteins

作　　者：赵妍[1] 刘晓林[1] 王若兰[1] 马玉洁[1] 杨俊[1] 

机构地区：[1]河南工业大学粮油食品学院,河南郑州450001

出　　处：《粮食与油脂》2014年第1期36-38,共3页Cereals & Oils

基　　金：国家高技术研究发展计划(863计划)项目(2012AA101705–2);公益性行业(农业)科研专项经费项目(201003077)

摘　　要：该研究采用傅里叶变换红外光谱(FTIR)技术测定不同温湿度微环境下储藏60 d和120 d的小麦蛋白质二级结构,并运用peakfit v4.12软件分析其变化规律。结果表明:原始小麦样品其蛋白质二级结构以β–折叠和无规则卷曲为主。在四种储藏微环境条件下,随储藏时间延长,小麦蛋白质二级结构总体均呈现α–螺旋结构明显减少、β–转角转换为β–折叠和无规则卷曲的趋势,其中α–螺旋也可能参与三者转化。说明在储藏期间小麦蛋白质螺旋结构被破坏;蛋白质二级结构由反转转化为折叠,蛋白质结构趋向稳定。对比四种储藏微环境,时间相同时,储藏于15℃,50%RH下的小麦蛋白质α–螺旋结构减少最小,有利于小麦品质保持。Protein secondary structure of wheat stored under different temperature and humidity conditions for 60 d and 120 d was analyzed by FTIR spectrometer,and the difference of protein secondary structure was analyzed by peakfit v4.12 software. Results showed that：the protein secondary structure of original wheat samples was mainlyβ-sheet and random coil. Under four different storage microenvironment and with the extension of storage time,the content ofα-helix reduced,whileβ-turn transformed toβ-sheet and random coils. Moreover,theα-helix might also be involved in the transformation of the three. During storage,the helix structure in wheat protein was destroyed,protein secondary structure by reversing into a folded,and the wheat protein secondary structure turned into stable. Compare the four kinds of storage microenvironment,α-helix structure reduced minimally（60 d and 120 d）in wheat which was stored under 15℃,50%RH,and under this storage condition ,wheat had the best quality.

关 键 词：小麦蛋白质 二级结构 红外光谱 储藏微环境 

分 类 号：TS201.21[轻工技术与工程—食品科学]