面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

李翠翠; 贾笑莉; 张丽; 郭赛赛; 孙薇; 陆啟玉

doi:10.12187/2024.06.001

面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

1. 郑州轻工业大学食品与生物工程学院, 河南郑州 450001;
2. 南阳理工学院张仲景康养与食品学院, 河南南阳 473000;
3. 南阳理工学院教师教育学院, 河南南阳 473000;
4. 河南工业大学粮油食品学院, 河南郑州 450001

作者简介: 李翠翠(1985—),女,河南省柘城县人,南阳理工学院副教授,博士,主要研究方向为面制品加工与研发。E-mail:licui8@yeah.net;

基金项目: 国家自然科学基金项目(31772002)
河南省高等教育重点科研项目(23A550017)
河南省科技攻关项目(212102110330)
南阳理工学院交叉科学研究项目(2024NGJC018)
南阳市科技发展计划项目(23JCQY2011)
中图分类号: TS213.2

Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products

1. College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China;
2. School of Zhang Zhongjing Health Care and Food, Nanyang Institute of Technology, Nanyang 473000, China;
3. School of Teachers Education, Nanyang Institute of Technology, Nanyang 473000, China;
4. School of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China
Received Date: 2024-01-02
Accepted Date: 2024-03-03
Available Online: 2024-12-15
CLC number: TS213.2

摘要: 二硫键(Disulphide Bond,S—S)是小麦面筋蛋白中最重要的共价键,可使蛋白质肽链的空间结构更为紧密,在一定条件下可与巯基(Sulfhydryl Group,—SH)相互转化。对近年来国内外有关面制品加工过程中小麦面筋蛋白—SH、S—S变化的研究进行综述,阐述—SH和S—S对面筋蛋白网络结构的影响机制,并从加工条件(温度变化、非热加工技术)和外源添加物(盐类物质、蛋白质、酶类、氧化剂、还原剂和巯基阻断剂)两方面论述面制品加工过程中小麦面筋蛋白—SH、S—S的变化机理。认为,小麦面筋蛋白S—S的形成通常有—SH的氧化和—SH/S—S的交换反应两种途径;冷藏、冷冻等低温条件会增加体系游离—SH的含量,使面筋蛋白网络结构的牢固性变差,适度的高温、高压、机械外力、真空等条件可促进蛋白质通过S—S发生交联,有利于面筋蛋白网络结构的形成;适量钾盐、小麦蛋白质二硫键异构酶、还原剂和巯基封闭剂可干扰游离—SH向S—S的转化,减缓面筋蛋白中S—S的形成,而适量钠盐、酸性蛋白酶、氧化酶和氧化剂则可促进S—S和三维聚合网络结构的形成。然而,目前相关研究对象主要集中于面条等主食面制品,且对其加工过程中—SH和S—S的动态分子结构变化的研究有限,有关天然功能因子与面筋蛋白—SH和S—S关系的研究也较少。未来应进一步扩大研究对象的种类,协同应用多种新技术解析面筋蛋白—SH和S—S的动态分子结构,重视功能性面制品的研发和化学机理探索,以期为研究—SH、S—S对面制品品质的影响机理提供参考,同时为基于—SH、S—S改良面制品品质、培育特种小麦等开拓新的研究思路。
- 巯基 /
- 二硫键 /
- 面制品 /
- 小麦面筋蛋白
Abstract: Disulphide bond (S—S) is the most important covalent bond in wheat gluten protein, enhancing the compactness of the spatial structure of protein peptide chains. Under certain conditions, S—S can be converted into sulfhydryl group (—SH). This paper reviewed recent domestic and international research on the changes of —SH and S—S in the processing of flour products elucidating the mechanisms of —SH and S—S in changing the network structure of gluten protein. The transforming mechanisms of —SH and S—S in wheat gluten protein in the processing of flour products were discussed from two aspects: processing conditions (temperature change, non-thermal processing technology) and additives (salts, proteins, enzymes, oxidants, reducing agents, and sulfhydryl blocking agents). It was believed that the formation of S—S in wheat gluten protein usually involves two pathways: —SH oxidation and —SH/S—S exchange reaction. Low temperature conditions such as refrigeration and freezing could increase the free —SH content of the system, leading to a decrease in the firmness of the gluten protein network. Moderate high temperature, high pressure, mechanical external force, vacuum and other conditions could promote protein cross-linking through S—S, which was conducive to the formation of the gluten protein network. External additives could alter the exchange reaction of —SH and S—S in gluten proteins. The moderate potassium salts, wheat protein disulfide isomerases, reducing agents, and thiol blocking agents could interfere with the conversion of free —SH to S—S, thereby slowing down the formation of S—S in gluten proteins. The moderate sodium salts, acidic proteases, oxidases, and oxidants could promote the formation of S—S and three-dimensional polymerization networks. However, current research objects mainly focus on staple flour products such as noodles, and the research on the dynamic molecular structure changes of —SH and S—S during the processing of facial products is limited. In addition, the research on the relationship between natural functional factors and —SH and S—S in gluten protein is also less. In the future, the variety of research objects should be further expanded, and multiple new technologies should be synergistically applied to analyze the dynamic molecular structure of —SH and S—S in gluten protein. More emphasis should be placed on the research and development of functional flour products and the exploration of chemical mechanisms. The review provided theoretical reference for deciphering the mechanism of —SH and S—S in influencing the quality of flour products and explored new research ideas for improving the quality of flour products and breeding special wheat varieties with —SH and S—S as the breakthroughs.
- sulfhydryl group /
- disulphide bond /
- flour product /
- wheat gluten protein
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沈阳化工大学材料科学与工程学院沈阳 110142

面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

作者简介: 李翠翠(1985—),女,河南省柘城县人,南阳理工学院副教授,博士,主要研究方向为面制品加工与研发。E-mail:licui8@yeah.net;

Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products

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通讯作者: 陈斌, bchen63@163.com

面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

作者简介:李翠翠(1985—),女,河南省柘城县人,南阳理工学院副教授,博士,主要研究方向为面制品加工与研发。E-mail:licui8@yeah.net

English Abstract

Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products

目录

面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

作者简介: 李翠翠(1985—),女,河南省柘城县人,南阳理工学院副教授,博士,主要研究方向为面制品加工与研发。E-mail:licui8@yeah.net;

Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products

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通讯作者: 陈斌, bchen63@163.com

面制品加工过程中小麦面筋蛋白巯基、二硫键变化的研究进展

作者简介:李翠翠(1985—),女,河南省柘城县人,南阳理工学院副教授,博士,主要研究方向为面制品加工与研发。E-mail:licui8@yeah.net

English Abstract

Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products

目录