Concentration-regulated fibrillation of peanut protein: Formation, structural characteristics, and emulsifying properties

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-04-09 DOI:10.1016/j.foodhyd.2025.111421

Qian Xu, Caiyun Cheng, Qingyun Li, Guangsu Zhu, Yunshan Wei, Kunlun Liu

{"title":"Concentration-regulated fibrillation of peanut protein: Formation, structural characteristics, and emulsifying properties","authors":"Qian Xu, Caiyun Cheng, Qingyun Li, Guangsu Zhu, Yunshan Wei, Kunlun Liu","doi":"10.1016/j.foodhyd.2025.111421","DOIUrl":null,"url":null,"abstract":"<div><div>This article investigates the structure and emulsification properties of peanut protein amyloid fibrils (PAFs) formed at pH 2.0 and different protein concentrations (PC). The findings demonstrated that with an escalation in the PC concentration (10−80 mg/mL), the conversion rate and β-sheet ratio of the fibrils significantly rose, suggesting that the increase in protein concentration promoted the formation of the fibrils. When the concentration was 10 mg/mL, large aggregates and a few short fibrils were formed; when the concentration was 40 mg/mL, more curved fibrils were formed; when the concentration is 60 mg/mL, long curved fibrils were formed; at higher concentrations (80 mg/mL), short and thick fibrils and rigid straight fibrils were formed. This indicates that the morphology of the fibrils formed under different PCs varies. Additionally, increasing the concentration of PC (10−60 mg/mL) rendered the PAF structure more stable, enhanced the thermal stability, and resulted in a higher emulsification activity index (EAI). When the protein concentration was higher (80 mg/mL), the EAI of the fibrils decreased. This study will intensify the exploration of the concentration-regulated protein fibrillation.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111421"},"PeriodicalIF":11.0000,"publicationDate":"2025-04-09","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/S0268005X25003819","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

This article investigates the structure and emulsification properties of peanut protein amyloid fibrils (PAFs) formed at pH 2.0 and different protein concentrations (PC). The findings demonstrated that with an escalation in the PC concentration (10−80 mg/mL), the conversion rate and β-sheet ratio of the fibrils significantly rose, suggesting that the increase in protein concentration promoted the formation of the fibrils. When the concentration was 10 mg/mL, large aggregates and a few short fibrils were formed; when the concentration was 40 mg/mL, more curved fibrils were formed; when the concentration is 60 mg/mL, long curved fibrils were formed; at higher concentrations (80 mg/mL), short and thick fibrils and rigid straight fibrils were formed. This indicates that the morphology of the fibrils formed under different PCs varies. Additionally, increasing the concentration of PC (10−60 mg/mL) rendered the PAF structure more stable, enhanced the thermal stability, and resulted in a higher emulsification activity index (EAI). When the protein concentration was higher (80 mg/mL), the EAI of the fibrils decreased. This study will intensify the exploration of the concentration-regulated protein fibrillation.

Abstract Image

查看原文本刊更多论文

花生蛋白的浓度调节颤动：形成、结构特征和乳化特性

研究了花生蛋白淀粉样原纤维（PAFs）在pH 2.0和不同蛋白浓度（PC）条件下的结构和乳化特性。结果表明，随着PC浓度的增加（10 ~ 80 mg/mL），原纤维的转化率和β-片比显著升高，表明蛋白质浓度的增加促进了原纤维的形成。当浓度为10 mg/mL时，形成大聚集体和少量短原纤维；当浓度为40 mg/mL时，形成更多弯曲的原纤维；浓度为60 mg/mL时，形成长而弯曲的原纤维；高浓度（80 mg/mL）可形成短而粗的原纤维和刚性的直原纤维。这表明在不同的pc条件下形成的原纤维形态不同。此外，增加PC浓度（10 ~ 60 mg/mL）使PAF结构更稳定，热稳定性增强，乳化活性指数（EAI）更高。当蛋白浓度较高（80 mg/mL）时，原纤维的EAI降低。本研究将加强对浓度调节蛋白颤的探索。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Food Hydrocolloids 工程技术-食品科技

CiteScore

19.90

自引率

14.00%

发文量

871

审稿时长

37 days

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.