分析与检测

微射流处理麦醇溶蛋白-芦丁复合物的拉曼光谱分析

  • 李春翼 ,
  • 王启明 ,
  • 雷小娟 ,
  • 赵吉春 ,
  • 雷琳 ,
  • 明建
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  • 1(西南大学 食品科学学院,重庆,400715)
    2(西南大学 食品贮藏与物流研究中心,重庆,400715)
第一作者:硕士研究生(明建教授为通信作者,E-mail:mingjian1972@163.com)

收稿日期: 2021-10-27

  修回日期: 2021-12-17

  网络出版日期: 2023-01-06

基金资助

国家重点研发计划专项课题(2016YFD0400203);国家自然科学基金面上项目(31471576)

Raman spectroscopy analysis of gliadin-rutin complex under dynamic high-pressure microfluidization

  • LI Chunyi ,
  • WANG Qiming ,
  • LEI Xiaojuan ,
  • ZHAO Jichun ,
  • LEI Lin ,
  • MING Jian
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  • 1(College of Food Science, Southwest University, Chongqing 400715, China)
    2(Research Center of Food Storage and Logistics, Southwest University, Chongqing 400715, China)

Received date: 2021-10-27

  Revised date: 2021-12-17

  Online published: 2023-01-06

摘要

为探究微射流条件下麦醇溶蛋白-芦丁复合物结构变化,以麦醇溶蛋白为对照,试样经过不同的微射流压力(0、40、80、120、160 MPa)处理2次后,通过拉曼光谱表征微射流对麦醇溶蛋白-芦丁复合物结构的影响,测定麦醇溶蛋白-芦丁复合物的游离巯基含量,氨基酸微环境,脂肪族残基变化,二级结构以及二硫键构象的变化。结果表明,麦醇溶蛋白与芦丁能发生相互作用,经过不同压力的微射流处理后复合物的游离巯基含量增加、氨基酸微环境趋于掩埋、复合物的α-螺旋、无规则卷曲含量减少,β-折叠、β-转角含量增加,t-g-t含量增加,相互作用力增强,结构趋于稳定。研究结果为麦醇溶蛋白的功能改性,结构修饰提供了新思路。

本文引用格式

李春翼 , 王启明 , 雷小娟 , 赵吉春 , 雷琳 , 明建 . 微射流处理麦醇溶蛋白-芦丁复合物的拉曼光谱分析[J]. 食品与发酵工业, 2022 , 48(24) : 233 -238 . DOI: 10.13995/j.cnki.11-1802/ts.029805

Abstract

To explore the structural changes of the gliadin-rutin complex under the condition of dynamic high-pressure microfluidization (DHPM), taking gliadin as the control, the sample was treated twice under different pressures (0, 40, 80, 120, and 160 MPa). The effect of DHPM on the structure of the gliadin-rutin complex was characterized by the Raman spectrum. And the free sulfhydryl content of the gliadin-rutin complex, amino acid microenvironment, secondary structure, and disulfide bond conformation was determined. Results showed that gliadin could interact with rutin. After DHPM treatment, the free sulfhydryl content of the complex increased, and the amino acid microenvironment tended to be buried. The content of α-helix as well as random coil decreased. However, β-sheet, β-turn, and t-g-t content increased, causing a stronger interaction among the molecules. The structure of the gliadin-rutin complex tended to be stable. The results provide a new idea for the functional modification and structural modification of gliadin.

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