Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature

Schreuders, Floor K.G.; Bodnár, Igor; Erni, Philipp; Boom, R.M.; Goot, A.J. van der

doi:10.1016/j.foodhyd.2019.105562

Cited by 42 publications

(31 citation statements)

References 24 publications

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“…It has also been described by Tolstoguzov that the water redistributes through phase separation, which leads to a water-rich and a water-poor phase. This phenomenon has already been reported in highly concentrated proteins structured via simple shear flow [ 65 , 66 ] and suggested for HME of pea protein isolate [ 86 ].…”

Section: Resultssupporting

confidence: 66%

“…Through the extrusion process, a water-rich dispersed phase was created, surrounded by a water-poor, i.e., protein-rich, continuous phase. The mechanism of water redistribution in highly concentrated, phase-separated biopolymer melts has been proposed by Tolstoguzov [ 44 ] from observations in biopolymer solutions and reported in highly concentrated biopolymer structures in shear cells [ 65 , 66 ]. However, this phenomenon was shown for multicomponent systems, i.e., mixtures of raw materials (SPI and wheat gluten and pea protein isolate and wheat gluten).…”

Section: Discussionmentioning

confidence: 99%

“…For this, the solubility in different solvent systems and the rheological properties of the proteins before and after extrusion are examined. Furthermore, the microstructure and water distribution of the extrudates are analyzed, as phases in phase-separated highly concentrated biopolymers have been shown to differ in their local water concentrations [ 65 , 66 ].…”

Section: Introductionmentioning

confidence: 99%

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High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

Wittek

Zeiler

Karbstein

et al. 2021

Foods

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The high moisture extrusion of plant proteins is well suited for the production of protein-rich products that imitate meat in their structure and texture. The desired anisotropic product structure of these meat analogues is achieved by extrusion at high moisture content (>40%) and elevated temperatures (>100 °C); a cooling die prevents expansion of the matrix and facilitates the formation of the anisotropic structure. Although there are many studies focusing on this process, the mechanisms behind the structure formation still remain largely unknown. Ongoing discussions are based on two very different hypotheses: structure formation due to alignment and stabilization of proteins at the molecular level vs. structure formation due to morphology development in multiphase systems. The aim of this paper is, therefore, to investigate the mechanism responsible for the formation of anisotropic structures during the high moisture extrusion of plant proteins. A model protein, soy protein isolate, is extruded at high moisture content and the changes in protein–protein interactions and microstructure are investigated. Anisotropic structures are achieved under the given conditions and are influenced by the material temperature (between 124 and 135 °C). Extrusion processing has a negligible effect on protein–protein interactions, suggesting that an alignment of protein molecules is not required for the structure formation. Instead, the extrudates show a distinct multiphase system. This system consists of a water-rich, dispersed phase surrounded by a water-poor, i.e., protein-rich, continuous phase. These findings could be helpful in the future process and product design of novel plant-based meat analogues.

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Section: Resultssupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

Wittek

Zeiler

Karbstein

et al. 2021

Foods

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“…The water distribution was hardly affected after a thermomechanical treatment (95-140 C and sheared at 39 s À1 for 15 min), as measured at room temperature (Dekkers, de Kort, et al 2016;Schreuders et al 2020). An alternative approach to determine the water partitioning is based on Flory-Huggins theory.…”

Section: Mixing and Hydrationmentioning

confidence: 94%

“…Clark et al (1983) proposed the use of Time-Domain Nuclear Magnetic Resonance (TD-NMR) to study the water partitioning between proteins. TD-NMR was used to study the water partitioning in hydrated mixtures of soy protein and gluten (Dekkers, de Kort, et al 2016), and pea protein and gluten (Schreuders et al 2020). Both studies found that gluten binds less water than soy or pea protein.…”

Section: Mixing and Hydrationmentioning

confidence: 99%

Thermo-mechanical processing of plant proteins using shear cell and high-moisture extrusion cooking

Cornet

Snel

Schreuders

et al. 2021

Critical Reviews in Food Science and Nutrition

129

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Use of soybean oil to modulate the gel properties of soybean protein isolation‐wheat gluten composite with or without CaCl₂

et al. 2023

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BACKGROUNDPlant protein is widely used in the study of animal protein substitutes and healthy sustainable products. The gel properties are crucial for the production of plant protein foods. Therefore, the present study investigated the use of soybean oil to modulate the gel properties of soybean protein isolation‐wheat gluten composite with or without CaCl2.RESULTSOil droplets filled protein network pores under the addition of soybean oil (1–2%). This resulted in an enhanced gel hardness and water holding capacity. Further addition of soybean oil (3–4%), oil droplets and some protein–oil compounds increased the distance between the protein molecule chain. The results of Fourier transform infrared spectroscopy and intermolecular interaction also showed that the disulfide bond and β‐sheet ratio decreased in the gel system, which damaged the overall structure of the gel network. Compared with the addition of 0 m CaCl2, salt ion reduced the electrostatic repulsion between proteins, and local protein cross‐linking was more intense at 0.005 m CaCl2 concentration. In the present study, structural properties and rheological analysis showed that the overall strength of the gel was weakened after the addition of CaCl2.CONCLUSIONThe presence of appropriate amount of soybean oil can fill the gel pores and improve the texture properties and network structure of soy protein isolate‐wheat gluten (SPI‐WG) composite gel. Excessive soybean oil may hinder protein–protein interaction and adversely affect protein gel. In addition, the presence or absence of CaCl2 significantly affected the gelling properties of SPI‐WG composite protein gels. © 2023 Society of Chemical Industry.

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Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature

Cited by 42 publications

References 24 publications

High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

Thermo-mechanical processing of plant proteins using shear cell and high-moisture extrusion cooking

Use of soybean oil to modulate the gel properties of soybean protein isolation‐wheat gluten composite with or without CaCl₂

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Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature

Cited by 42 publications

References 24 publications

High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

High Moisture Extrusion of Soy Protein: Investigations on the Formation of Anisotropic Product Structure

Thermo-mechanical processing of plant proteins using shear cell and high-moisture extrusion cooking

Use of soybean oil to modulate the gel properties of soybean protein isolation‐wheat gluten composite with or without CaCl2

Contact Info

Product

Resources

About

Use of soybean oil to modulate the gel properties of soybean protein isolation‐wheat gluten composite with or without CaCl₂