{"title":"Regulation of disulfide bond cleavage on the physicochemical and digestive properties of EGCG-gluten covalent complexes","authors":"Qiu-Yue Ma , Qian-Da Xu , Nan Chen , Wei-Cai Zeng","doi":"10.1016/j.foodhyd.2025.111724","DOIUrl":null,"url":null,"abstract":"<div><div>Disulfide bond critically govern gluten structure and its covalent interactions with polyphenols, ultimately determining gluten-polyphenol complex properties. This study investigated how disulfide bond cleavage modulates gluten structure, enhances epigallocatechin gallate (EGCG)-gluten covalent binding, and regulates the physicochemical/digestive properties of their complexes. Sodium metabisulfite treatment (0–25 mM treatment) induced disulfide bonds cleavage, which promoted the structural unfolding and exposed reactive groups for covalent binding with EGCG. With analysis of particle size, fluorescence spectroscopy, fourier-transform infrared spectroscopy, and thermogravimetric analysis, disulfide bond cleavage significantly reduced the particle size (from 124.5 to 62.26 μm) of gluten, altered the secondary (α-helix decreased from 23.4 % to 15.1 %, β-sheet from 32.8 % to 23.7 %) and tertiary structures of gluten, increased its surface hydrophobicity and enhanced its binding efficiency (from 51.98 % to 62.02 %) with EGCG. With increase of disulfide bond cleavage, EGCG-gluten covalent complexes exhibited enhanced thermal, pH, and oxidation stability, along with strong antioxidant activity. In addition, the disulfide bond cleavage of gluten inhibited the premature releasing and degradation of EGCG from covalent complexes during the digestion process, which was beneficial for improving the bioaccessibility of EGCG. All results suggest that the disulfide bond cleavage of gluten improve the physicochemical and digestive properties of EGCG-gluten covalent complexes, which provides a potential approach to regulate the properties of proteins-polyphenols covalent complexes as delivery systems of active compounds for functional foods and nutraceuticals.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111724"},"PeriodicalIF":11.0000,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25006848","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
Disulfide bond critically govern gluten structure and its covalent interactions with polyphenols, ultimately determining gluten-polyphenol complex properties. This study investigated how disulfide bond cleavage modulates gluten structure, enhances epigallocatechin gallate (EGCG)-gluten covalent binding, and regulates the physicochemical/digestive properties of their complexes. Sodium metabisulfite treatment (0–25 mM treatment) induced disulfide bonds cleavage, which promoted the structural unfolding and exposed reactive groups for covalent binding with EGCG. With analysis of particle size, fluorescence spectroscopy, fourier-transform infrared spectroscopy, and thermogravimetric analysis, disulfide bond cleavage significantly reduced the particle size (from 124.5 to 62.26 μm) of gluten, altered the secondary (α-helix decreased from 23.4 % to 15.1 %, β-sheet from 32.8 % to 23.7 %) and tertiary structures of gluten, increased its surface hydrophobicity and enhanced its binding efficiency (from 51.98 % to 62.02 %) with EGCG. With increase of disulfide bond cleavage, EGCG-gluten covalent complexes exhibited enhanced thermal, pH, and oxidation stability, along with strong antioxidant activity. In addition, the disulfide bond cleavage of gluten inhibited the premature releasing and degradation of EGCG from covalent complexes during the digestion process, which was beneficial for improving the bioaccessibility of EGCG. All results suggest that the disulfide bond cleavage of gluten improve the physicochemical and digestive properties of EGCG-gluten covalent complexes, which provides a potential approach to regulate the properties of proteins-polyphenols covalent complexes as delivery systems of active compounds for functional foods and nutraceuticals.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.