Effect of Heat Treatment on the Molecular and Functional Properties of Pea Protein Isolate

IF 3.2 4区 农林科学 Q2 FOOD SCIENCE & TECHNOLOGY Food Biophysics Pub Date : 2025-03-31 DOI:10.1007/s11483-025-09954-x
Rui Liu, Camilla P. Frederiksen, Trine R. Rasmussen, Serafim Bakalis, Poul Erik Jensen, Svemir Rudić, Heloisa N. Bordallo, Ourania Gouseti
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Abstract

This work aimed at understanding the effect of heat treatment on the properties and functionalities of pea protein isolate (PPI). PPI was characterised using thermogravimetric methods coupled with evolved gas analysis, differential scanning calorimetry, and X-Ray powder diffraction. As water is an integral component in determining protein properties, inelastic neutron scattering was further used to study water populations in the PPI powder. Hydration time was identified as key in determining solubility. Heat treatment resulted in partially denatured, more soluble, less thermodynamically stable, and less crystalline PPI compared to the control. Heating, often associated with protein aggregation and particle size increase, was found to reduce PPI particle sizes, which was attributed to the disruption of non-covalent interactions. During emulsification, these features enhanced formation of smaller drops, stable against coalescence. Compared to the control, the heat-treated PPI produced emulsions with increased shear thinning (power law index of 0.6 compared to 0.9) and consistency (≈10 times higher), as it has been previously reported for emulsions with fine, compared to coarse, droplets. Acid-induced gels of the heat-treated PPI were ≈4 times more elastic (G’) compared to the control. Overall, this work contributes towards the design of plant-based foods with predictable characteristics by understanding the link between protein physicochemical properties and food functionality.

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热处理对豌豆分离蛋白分子和功能特性的影响
本工作旨在了解热处理对豌豆分离蛋白(PPI)性质和功能的影响。用热重法结合演化气分析、差示扫描量热法和x射线粉末衍射对PPI进行了表征。由于水是决定蛋白质性质的重要组成部分,我们进一步利用非弹性中子散射技术研究了PPI粉末中的水族。水化时间是决定溶解度的关键因素。与对照组相比,热处理导致部分变性,可溶性更高,热力学稳定性更差,结晶PPI更少。加热通常与蛋白质聚集和颗粒大小增加有关,发现PPI颗粒大小减小,这归因于非共价相互作用的破坏。在乳化过程中,这些特征促进了小液滴的形成,防止聚结。与对照组相比,经过热处理的PPI产生的乳剂具有更高的剪切稀化(幂律指数为0.6,而不是0.9)和稠度(≈10倍),正如之前报道的那样,乳剂具有细滴,而不是粗滴。经过热处理的PPI酸致凝胶的弹性(G′)是对照组的约4倍。总的来说,这项工作有助于通过理解蛋白质物理化学性质和食品功能之间的联系来设计具有可预测特征的植物性食品。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Food Biophysics
Food Biophysics 工程技术-食品科技
CiteScore
5.80
自引率
3.30%
发文量
58
审稿时长
1 months
期刊介绍: Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell. A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.
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