Xu Zhang , Hekai Zhao , Yao Lu , Baokun Qi , Yang Li
{"title":"Study on the mechanism of riboflavin/UV induced soy protein nanofibrils hydrogel by photo crosslinking","authors":"Xu Zhang , Hekai Zhao , Yao Lu , Baokun Qi , Yang Li","doi":"10.1016/j.foodhyd.2025.111671","DOIUrl":null,"url":null,"abstract":"<div><div>Fibrillar modification significantly enhanced the functional properties of soy protein nanofibrils (SPF). Through acid-heat induction, this study successfully converted soy protein isolate (SPI) into SPF and systematically investigated the gelation mechanism of riboflavin (RF)/UV-induced SPF photo-crosslinked hydrogels. The results demonstrated that RF actively participated in the crosslinking reaction, and fibrillar modification significantly improved the binding ability of SPI with RF. Isothermal titration calorimetry (ITC) revealed that fibrillar modification altered the thermodynamics of the SPI/RF binding, shifting the reaction from endothermic to exothermic, with the binding driving force transitioning from hydrophobic interactions to hydrogen bonding. After UV irradiation at a riboflavin concentration of 0.5 mM, both SPI and SPF samples exhibited optimal rheological properties. Notably, the SPF/RF system was able to stably form a gel, with its storage modulus increasing by 74-fold and 25-fold compared to the SPI/RF system and the native SPF sample, respectively. This enhancement indicates the formation of a more continuous three-dimensional network structure, wherein riboflavin functions as a photocatalyst. Circular dichroism analysis indicated that photo crosslinking did not significantly alter the protein's secondary structure. Additionally, Raman spectroscopy analysis showed a reduction in the characteristic peaks of phenylalanine (970−1055 cm<sup>−1</sup>) and tryptophan (756 cm<sup>−1</sup>) after photo crosslinking, suggesting that synergistic interactions with tyrosine contributed to the formation of the crosslinking network. This study provides a theoretical foundation for the design of light-responsive plant protein-based materials and broadens the application prospects of SPF.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111671"},"PeriodicalIF":11.0000,"publicationDate":"2025-06-21","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/S0268005X25006319","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
Fibrillar modification significantly enhanced the functional properties of soy protein nanofibrils (SPF). Through acid-heat induction, this study successfully converted soy protein isolate (SPI) into SPF and systematically investigated the gelation mechanism of riboflavin (RF)/UV-induced SPF photo-crosslinked hydrogels. The results demonstrated that RF actively participated in the crosslinking reaction, and fibrillar modification significantly improved the binding ability of SPI with RF. Isothermal titration calorimetry (ITC) revealed that fibrillar modification altered the thermodynamics of the SPI/RF binding, shifting the reaction from endothermic to exothermic, with the binding driving force transitioning from hydrophobic interactions to hydrogen bonding. After UV irradiation at a riboflavin concentration of 0.5 mM, both SPI and SPF samples exhibited optimal rheological properties. Notably, the SPF/RF system was able to stably form a gel, with its storage modulus increasing by 74-fold and 25-fold compared to the SPI/RF system and the native SPF sample, respectively. This enhancement indicates the formation of a more continuous three-dimensional network structure, wherein riboflavin functions as a photocatalyst. Circular dichroism analysis indicated that photo crosslinking did not significantly alter the protein's secondary structure. Additionally, Raman spectroscopy analysis showed a reduction in the characteristic peaks of phenylalanine (970−1055 cm−1) and tryptophan (756 cm−1) after photo crosslinking, suggesting that synergistic interactions with tyrosine contributed to the formation of the crosslinking network. This study provides a theoretical foundation for the design of light-responsive plant protein-based materials and broadens the application prospects of SPF.
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.