Fabrication of pea protein isolate-stabilized oil-in-water emulsions with high freeze-thaw stability: Effect of high intensity ultrasonic on emulsions and interfacial protein structure
{"title":"Fabrication of pea protein isolate-stabilized oil-in-water emulsions with high freeze-thaw stability: Effect of high intensity ultrasonic on emulsions and interfacial protein structure","authors":"","doi":"10.1016/j.foodhyd.2024.110484","DOIUrl":null,"url":null,"abstract":"<div><p>The poor freeze-thaw stability of plant protein-based emulsions posed a major challenge for their application in the cold chain foods. The present study successfully prepared oil-in-water emulsions stabilized solely with pea protein isolate (PPI) with excellent freeze-thaw stability using a facile high intensity ultrasonic (HIU)-assisted method. The optimized emulsion can endure three freeze-thaw cycles without stratification or oil leakage, maintaining oil droplet sizes at the nanometer scale. Furthermore, changes of interfacial protein structure induced by HIU were systematically investigated to reveal the stabilizing mechanism. The freeze-thaw stability of emulsions treated under varying intensities was evaluated based on changes in the appearance and oil drop size distribution. The results showed that the oil drop size of emulsions decreased from micron to nanometer and the freeze-thaw stability was significantly enhanced with the increase of HIU intensity. The emulsion exhibited optimized freeze-thaw stability under 800W. Subsequently, the effect of HIU on the structure of interfacial protein was analyzed through SDS-PAGE, –SH/S–S contents, UV spectrum, surface hydrophobicity, protein adsorption percentage, emulsifying activity and interfacial dilatational rheology. It was found that HIU triggered crosslinking of disulfide bonds among interfacial PPI molecules and enhanced the strength of the interface layer. Additionally, HIU promoted the unfolding of interfacial PPI structure, resulting in the improvement of surface hydrophobicity, emulsifying activity, and interfacial adsorption percentage of PPI. The study demonstrated the feasibility of using HIU to improve the freeze-thaw stability of oil-in-water emulsions stabilized with PPI and provided references for the fabricating of plant protein-based frozen emulsion foods.</p></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":null,"pages":null},"PeriodicalIF":11.0000,"publicationDate":"2024-07-30","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/S0268005X24007586","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
The poor freeze-thaw stability of plant protein-based emulsions posed a major challenge for their application in the cold chain foods. The present study successfully prepared oil-in-water emulsions stabilized solely with pea protein isolate (PPI) with excellent freeze-thaw stability using a facile high intensity ultrasonic (HIU)-assisted method. The optimized emulsion can endure three freeze-thaw cycles without stratification or oil leakage, maintaining oil droplet sizes at the nanometer scale. Furthermore, changes of interfacial protein structure induced by HIU were systematically investigated to reveal the stabilizing mechanism. The freeze-thaw stability of emulsions treated under varying intensities was evaluated based on changes in the appearance and oil drop size distribution. The results showed that the oil drop size of emulsions decreased from micron to nanometer and the freeze-thaw stability was significantly enhanced with the increase of HIU intensity. The emulsion exhibited optimized freeze-thaw stability under 800W. Subsequently, the effect of HIU on the structure of interfacial protein was analyzed through SDS-PAGE, –SH/S–S contents, UV spectrum, surface hydrophobicity, protein adsorption percentage, emulsifying activity and interfacial dilatational rheology. It was found that HIU triggered crosslinking of disulfide bonds among interfacial PPI molecules and enhanced the strength of the interface layer. Additionally, HIU promoted the unfolding of interfacial PPI structure, resulting in the improvement of surface hydrophobicity, emulsifying activity, and interfacial adsorption percentage of PPI. The study demonstrated the feasibility of using HIU to improve the freeze-thaw stability of oil-in-water emulsions stabilized with PPI and provided references for the fabricating of plant protein-based frozen emulsion foods.
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.