{"title":"Role of phosphate modification in enhancing ovalbumin fibril formation and functionality: Insights into molecular interactions and structural dynamics","authors":"Yu Xun , Zhouyi Xiong , Yongtian Song , Yuqaing Zhao , Hanguo Xiong","doi":"10.1016/j.ifset.2025.103992","DOIUrl":null,"url":null,"abstract":"<div><div>Amyloid fibrils from proteins have garnered significant attention from researchers due to their outstanding functional properties. This study aims to in<em>v</em>estigate the effects of different sodium tripolyphosphate (STPP) concentrations (0.4 %, 4.0 %, and 8.0 %, <em>w</em>/<em>v</em>) on the formation and functional properties of ovalbumin (OVA) amyloid fibrils under heating conditions. Thioflavin T (ThT) assay revealed that the addition of STPP significantly accelerated the fibril formation potential. The fibril formation mechanism was explored through circular dichroism (CD), hydrophobic interaction, zeta potential, and Fourier transform infrared (FTIR) spectral analyses. Hydrophobic interactions and electrostatic repulsion were found to be the main driving forces for fibril formation of STPP-modified OVA (POVA). TEM results showed that STPP concentration was the key factor for regulating the morphology of OVA fibrils, with filamentous and worm-like fibrils for 0.4 % and 4.0 % POVA, respectively, while aggregated fibrils for 8.0 % POVA, due to the decrease of hydrophobic interaction and electrostatic repulsion. The 4.0 % POVA fibrils had the best emulsification capacity and foaming properties. The emulsion stabilized with 4.0 % POVA was the most stable. Overall, this study elucidated the potential formation mechanism of POVA fibrils, providing an environmentally friendly idea for preparation of OVA fibrils. Meanwhile, it had great potential as delivery systems for food constituents.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"102 ","pages":"Article 103992"},"PeriodicalIF":6.3000,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Innovative Food Science & Emerging Technologies","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1466856425000761","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Amyloid fibrils from proteins have garnered significant attention from researchers due to their outstanding functional properties. This study aims to investigate the effects of different sodium tripolyphosphate (STPP) concentrations (0.4 %, 4.0 %, and 8.0 %, w/v) on the formation and functional properties of ovalbumin (OVA) amyloid fibrils under heating conditions. Thioflavin T (ThT) assay revealed that the addition of STPP significantly accelerated the fibril formation potential. The fibril formation mechanism was explored through circular dichroism (CD), hydrophobic interaction, zeta potential, and Fourier transform infrared (FTIR) spectral analyses. Hydrophobic interactions and electrostatic repulsion were found to be the main driving forces for fibril formation of STPP-modified OVA (POVA). TEM results showed that STPP concentration was the key factor for regulating the morphology of OVA fibrils, with filamentous and worm-like fibrils for 0.4 % and 4.0 % POVA, respectively, while aggregated fibrils for 8.0 % POVA, due to the decrease of hydrophobic interaction and electrostatic repulsion. The 4.0 % POVA fibrils had the best emulsification capacity and foaming properties. The emulsion stabilized with 4.0 % POVA was the most stable. Overall, this study elucidated the potential formation mechanism of POVA fibrils, providing an environmentally friendly idea for preparation of OVA fibrils. Meanwhile, it had great potential as delivery systems for food constituents.
期刊介绍:
Innovative Food Science and Emerging Technologies (IFSET) aims to provide the highest quality original contributions and few, mainly upon invitation, reviews on and highly innovative developments in food science and emerging food process technologies. The significance of the results either for the science community or for industrial R&D groups must be specified. Papers submitted must be of highest scientific quality and only those advancing current scientific knowledge and understanding or with technical relevance will be considered.