Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation

Mession, Jean-Luc; Chihi, Mohammed Lazhar; Sok, Nicolas; Saurel, Rémi

doi:10.1016/j.foodhyd.2014.11.025

Cited by 157 publications

(91 citation statements)

References 24 publications

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“…They did however not give any pH values at which the structuring occurred. Mession et al, 2015 reported gel-points at pH 6.7 for pea protein acidified with glucono-δ-lactone but offered no reference to this value being distinctly above the isoelectric point. Some explanations can be found in Grygorczyk & Corredig, 2013, who previously reported a gel-point at pH 6.29 ± 0.05 for soy-protein acidified via fermentation.…”

Section: Structure-formation During Fermentationmentioning

confidence: 99%

“…In contrast, the structuring behaviour and gel properties upon fermentation of pea protein alone have not been investigated in detail. The few studies covering pea protein used glucono-δ-lactone for acidification (Ben-Harb et al, 2017;Mession, Chihi, Sok, & Saurel, 2015). However it is well described in literature that kinetics of acidification and structure formation during microbial fermentation may differ from kinetics when using glucono-δ-lactone (Grygorczyk & Corredig, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Structure formation and rheological properties of pea protein-based gels

Klost

Drusch

2019

Food Hydrocolloids

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Nutritional recommendations for the elderly, but also the general public, include incorporation of plant proteins in the diet, an increase in the intake of Ω-3 fatty acids and an increase in intake of dietary fibre. Protein structure and structuring behaviour of plant proteins differ from that of milk proteins. Therefore, the aim of the presented study was to characterise the structuring process and resulting structure of yoghurt-style gels containing 10% pea protein with and without addition of nutritionally recommended ingredients like rapeseed-oil and/or commercial oat fibre. Rheological measurements were combined with microscopy for sample characterisation. Generally, all studied formulations were able to form acid induced gels via fermentation. The acidification led to a two-phase gelation process resulting in thick gels that showed mainly weak rheological behaviour. Supplementation with oil and/or fibre resulted in an increase of the relative concentration of pea protein in the aqueous phase and led to a strong increase in the complex shear modulus |G*| as well as the maximum structuring velocity d|G*|/dt. These effects need to be considered when tailoring yoghurt-style gels with high consumer acceptance.

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Section: Structure-formation During Fermentationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structure formation and rheological properties of pea protein-based gels

Klost

Drusch

2019

Food Hydrocolloids

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“…In many cases, processing of pea protein ingredients involves a thermal treatment step, which can lead to the formation of a gel structure if the protein concentration is above a minimum level (Shand, Ya, Pietrasik, & Wanasundara, ; Sun & Arntfield, ). Other methods used to obtain pea based gels include enzymatic treatments (Djoullah, Husson, & Saurel, ) and acid‐induced gelation (Mession, Chihi, Sok, & Saurel, ). During the heat denaturation of pea proteins, a pronounced “cooked” flavor is formed (Malcolmson et al, ), which is undesirable to many consumers.…”

Section: Introductionmentioning

confidence: 99%

“…. Other methods used to obtain pea based gels include enzymatic treatments (Djoullah, Husson, & Saurel, 2017) and acid-induced gelation (Mession, Chihi, Sok, & Saurel, 2015). During the heat denaturation of pea proteins, a pronounced "cooked" flavor is formed (Malcolmson et al, 2014), which is undesirable to many consumers.…”

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confidence: 99%

High pressure structuring of pea protein concentrates

Sim

Karwe

Moraru

2019

J Food Process Engineering

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This work demonstrates the use of high pressure processing (HPP) to induce structural modifications in pea protein concentrates (PPC). Reconstituted PPC with 8–24 g protein /100 g water were subjected to HPP at 250–550 MPa for 15 min, at 20–33°C, or heat treatments at 95°C for 15 min. Structural changes were investigated using dynamic rheology, scanning electron microscopy, differential scanning calorimetry, and mid‐infrared spectroscopy. Gel formation occurred at 16 g protein /100 g water concentration and 250 MPa for the HPP‐treated samples, and at 12 g protein /100 g water concentration for the heat‐treated samples. Gel strength increased with both pressure level and protein concentration. Heat‐treated samples exhibited greater gel strength than pressure‐treated samples at the same protein concentration. A greater extent of protein denaturation, aggregation, and network formation occurred with increasing pressure level, due to protein tertiary and quaternary conformation changes. Starch granules present in PPC retained their structure and were not gelatinized even at 550 MPa. These findings can be used to create novel pea protein products with interesting structures and superior sensory and nutritional properties. Practical Applications This work shows that a range of unique pea‐based products, such as puddings or tofu analogs, can be created by low temperature HPP treatment of pea protein concentrates at different pressure levels and protein concentrations. This process has the potential to better preserve the organoleptic and nutritional properties of the final products compared to traditional, heat based processing methods. These findings can be also extended to create other pulse protein products using high pressure processing.

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“…Albumin aggregates (AA) were obtained as described in the previous work concerning pea-Glob (Chihi, Mession, Sok, & Saurel, 2016;Mession, Chihi, Sok, & Saurel, 2015). First, 3% (w/v) albumin dispersions were prepared in distilled water at different pHs (3, 5, or 7) and stirred 12 hr at +6°C to complete hydration.…”

Section: Preparation Of Albumin Aggregates (Aa)mentioning

confidence: 99%

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

Djemaoune

Cases

Saurel

2019

Journal of Food Science

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The effect of dynamic high‐pressure treatment, also named microfluidization, on the surface properties of thermal pea albumin aggregates (AA) and their foaming ability was investigated at pH 3, 5, and 7. The solubility of albumin particles was not affected by the increase in microfluidization pressure from 70 to 130 MPa. Particle charge depended only on the pH, whereas protein surface hydrophobicity was stable at pH 5, decreased at pH 3, but increased at pH 7 after microfluidization treatment and with the applied pressure. Surface tension of AA measured at air/water interface was favorably affected by the microfluidization treatment at each pH preferentially due to size reduction and increased flexibility of protein particles. The foaming capacity and stability of AA depended on the pH conditions and the microfluidization treatment. The high‐pressure treatment had little influence in foaming properties at acidic pHs, probably related to a more compact form of AA at these pHs. At neutral pH, the foaming properties of pea AA were strongly influenced by their surface properties and size associated with significant modifications in AA structure with microfluidization. Changes in albumin aggregate characteristics with pH and microfluidization pressure are also expected to modulate other techno‐functional properties, such as emulsifying property. Practical Application Albumins are known for their interesting nutritional values because they are rich in essential amino acids. This fraction is not currently marketed as a protein isolate for human consumption, but can be considered as a potential new vegetable protein ingredient. This document demonstrated that heat treatment or dynamic high‐pressure technology can control the foaming properties of this protein for possible use in expanded foods.

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Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation

Cited by 157 publications

References 24 publications

Structure formation and rheological properties of pea protein-based gels

Structure formation and rheological properties of pea protein-based gels

High pressure structuring of pea protein concentrates

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

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