储藏微环境对小麦蛋白质二级结构影响.pdfVIP

1014ls01-11 36 粮食与油脂 2014 年第 27 卷第 1 期 储藏微环境对小麦蛋白质二级结构影响 赵　妍，刘晓林，王若兰，马玉洁，杨　俊 （河南工业大学粮油食品学院，　河南郑州　450001 ） 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 α β β 蛋白质二级结构总体均呈现 – 螺旋结构明显减少、– 转角转换为 – 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 ℃， α 50% RH 下的小麦蛋白质 – 螺旋结构减少最小，有利于小麦品质保持。 关键词：小麦蛋白质；二级结构；红外光谱；储藏微环境 Influence of storage microenvironment to the secondary structure in wheat proteins ZHAO Yan ，LIU Xiao-lin ，WANG Ruo-lan ，MA Yu-jie ，YANG Jun （College of Food Science and Technology ，Henan University of Technology ，Zhengzhou 450001 ，Henan ，China ） Abstract ：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 mainly β–sheet and random coil. Under four different storage microenvironment and with the extension of storage time ，the content of α–helix reduced ，while β–turn transformed to β–sheet and random coils. Moreover ，the α–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 α stable. Compare