Mixing commercial plant proteins compromises the mechanical properties of heat-set gels

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-09-16 DOI:10.1016/j.foodhyd.2025.111993

Senna W.P.M. Janssen , Meike Lokker , Laurice Pouvreau , Renko J. de Vries

{"title":"Mixing commercial plant proteins compromises the mechanical properties of heat-set gels","authors":"Senna W.P.M. Janssen , Meike Lokker , Laurice Pouvreau , Renko J. de Vries","doi":"10.1016/j.foodhyd.2025.111993","DOIUrl":null,"url":null,"abstract":"<div><div>Mixing plant proteins can be a strategy to improve the nutritional value, availability, costs, flavour and functionality of plant proteins in food products. However, a challenge is that the properties of mixed gels cannot yet be predicted by the characteristics of the protein sources alone. To address this challenge, we here systematically study mixed heat-set gels for two commercial plant protein isolates. Separate stock dispersions of two commercial plant protein isolates (pea (PPI) and fava bean (FBPI)) that differ in gelling properties, were created under various conditions: 10–15 % w/w protein, pH 6 and 7, with or without homogenization (500 bar_2cycles) and mixed at different ratios (4:0, 3:1, 2:2, 1:3 and 0:4). We observed mainly anti-synergistic mixing behaviour: shear moduli and fracture stress were lower for mixed gels than for the pure counterparts. Microstructural analysis did not reveal any phase separation, suggesting the proteins were not incompatible. Lowering the pH from pH 7 to pH 6 led to less anti-synergistic mixing behaviour, but overall, large deformation properties decreased. Our results demonstrate that the possible benefits of mixing must be balanced with the impact of mixing on functionality.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111993"},"PeriodicalIF":11.0000,"publicationDate":"2025-09-16","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/S0268005X25009531","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

Mixing plant proteins can be a strategy to improve the nutritional value, availability, costs, flavour and functionality of plant proteins in food products. However, a challenge is that the properties of mixed gels cannot yet be predicted by the characteristics of the protein sources alone. To address this challenge, we here systematically study mixed heat-set gels for two commercial plant protein isolates. Separate stock dispersions of two commercial plant protein isolates (pea (PPI) and fava bean (FBPI)) that differ in gelling properties, were created under various conditions: 10–15 % w/w protein, pH 6 and 7, with or without homogenization (500 bar_2cycles) and mixed at different ratios (4:0, 3:1, 2:2, 1:3 and 0:4). We observed mainly anti-synergistic mixing behaviour: shear moduli and fracture stress were lower for mixed gels than for the pure counterparts. Microstructural analysis did not reveal any phase separation, suggesting the proteins were not incompatible. Lowering the pH from pH 7 to pH 6 led to less anti-synergistic mixing behaviour, but overall, large deformation properties decreased. Our results demonstrate that the possible benefits of mixing must be balanced with the impact of mixing on functionality.

Abstract Image

查看原文本刊更多论文

混合商业植物蛋白会损害热固化凝胶的机械性能

混合植物蛋白是一种提高食品中植物蛋白的营养价值、可用性、成本、风味和功能的策略。然而，一个挑战是，混合凝胶的性质还不能仅通过蛋白质来源的特征来预测。为了解决这一挑战，我们在这里系统地研究了两种商业植物蛋白分离物的混合热固凝胶。两种商业植物蛋白分离物（豌豆（PPI）和蚕豆（FBPI））在不同的条件下(10 - 15% w/w蛋白，pH 6和7，均质或不均质（500 bar_2cycles），并以不同的比例（4:0,3:1,2:2,1:3和0:4）混合，制备了胶凝性能不同的单独原液分散体。我们观察到的主要是反协同混合行为：混合凝胶的剪切模量和断裂应力低于纯凝胶。微观结构分析没有发现任何相分离，表明蛋白质不是不相容的。当pH值从pH 7降低到pH 6时，抗增效混合行为减少，但总体而言，大变形性能下降。我们的结果表明，混合可能带来的好处必须与混合对功能的影响相平衡。

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.