摘要
为探究超声条件下麦醇溶蛋白与芦丁的相互作用,将麦醇溶蛋白(对照)和芦丁-麦醇溶蛋白复合物经过不同的超声功率(0、150、300、450、600 W)处理20 min后,通过内源荧光光谱、同步荧光光谱、紫外扫描光谱检测超声功率对麦醇溶蛋白与芦丁相互作用的影响,测定麦醇溶蛋白与芦丁复合物的表面疏水性、游离巯基含量、热稳定性以及微观结构的变化。结果表明,不同超声功率处理会影响麦醇溶蛋白与芦丁之间的相互作用。与未超声的复合物相比,超声后芦丁-麦醇溶蛋白复合物的表面疏水性和游离巯基含量均增加,最高分别达到(37.00±0.47)μg、(10.59±0.42)μmol/g。加入芦丁后,复合物的热稳定性提高,呈现疏松多孔的微观结构。研究结果可为麦醇溶蛋白的功能改性、结构修饰提供参考。
In order to investigate the interaction between gliadin from wheat and rutin under ultrasonic condition,the effect of ultrasonic power on the interaction between wheat gliadin and rutin was characterized by intrinsic fluorescence spectroscopy,synchronous fluorescence spectroscopy and ultraviolet(UV)absorption spectroscopy after 20-minute treatment with different ultrasonic powers(0,150,300,450,and 600 W).The changes in the surface hydrophobicity,free sulfhydryl group content,thermal stability and microstructure of gliadin-rutin complex were determined.The results showed that the interaction between gliadin and rutin was affected by ultrasonic treatment.Besides,ultrasonic treatment increased the surface hydrophobicity and free sulfhydryl group content of the complex up to(37.00±0.47)μg and(10.59±0.42)μmol/g compared to the untreated control,respectively.The complex had better thermal stability than did gliadin when treated with the same ultrasonic power,and the treated complex exhibited a loose and porous microstructure.This study provides a new way for the functional and structural modification of gliadin from wheat.
作者
薛艾莲
李春翼
王启明
张驰
雷小娟
赵吉春
曾凯芳
明建
XUE Ailian;LI Chunyi;WANG Qiming;ZHANG Chi;LEI Xiaojuan;ZHAO Jichun;ZENG Kaifang;MING Jian(College of Food Science,Southwest University,Chongqing 400715,China;Research Center of Food Storage and Logistics,Southwest University,Chongqing 400715,China)
出处
《食品科学》
EI
CAS
CSCD
北大核心
2022年第7期45-51,共7页
Food Science
基金
“十三五”国家重点研发计划重点专项(2016YFD0400203)
国家自然科学基金面上项目(31771970)。