Gelation behaviors of denaturated pea albumin and globulin fractions during transglutaminase treatment

Djoullah, Attaf; Husson, Florence; Saurel, Rémi

doi:10.1016/j.foodhyd.2017.11.005

Cited by 65 publications

(33 citation statements)

References 29 publications

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“…Usually, the goal of crosslinking is to improve the textural properties of the protein by building up the polypeptides into stronger structures. TG (EC 2.3.2.13) is the only commercially available food‐grade cross‐linking enzyme and it been reported to improve texture, viscosity, ES, gelation, foam and increase hydrophobicity properties of food proteins (Djoullah, Husson, & Saurel, 2018; Glusac, Isaschar‐Ovdat, & Fishman, 2020; Nivala, Mäkinen, Kruus, Nordlund, & Ercili‐Cura, 2017; Sun, & Arntfield, 2011a). Sun & Arntfield (2011a), reported that TG increased the gel strength of PPI 8 times and SPI gel by 2 times in comparison to the gel made from untreated protein; gel strength also increased with higher TG levels.…”

Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

342

136

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The market trend towards plant‐based protein has seen a significant increase in the last decade. This trend has been projected to continue in the coming years because of the strong factors of sustainability and less environmental impact associated with the production of plant‐based protein compared to animal, aside from other beneficial health claims and changes in consumers' dietary lifestyles. In order to meet market demand, there is a need to have plant‐based protein ingredients that rival or have improved quality and functionality compared to the traditional animal protein ingredients they may replace. In this review article, we present a detailed and concise summary of the functionality challenges of some plant protein ingredients with associated physical, chemical, and biological processing techniques (traditional and emerging technologies) that have been attempted to enhance them. We cataloged the differences between several studies that seek to address the functionality challenges of selected plant‐based protein ingredients without overtly commenting on a general technique that addresses the functionality of all plant‐based protein ingredients. Additionally, we elucidated the chemistry behind some of these processing techniques and how they modify the protein structure for improved functionality. Although, many food industries are shifting away from chemical modification of proteins because of the demand for clean label product and the challenge of toxicity associated with scale‐up of this technique, so physical and biological techniques are widely being adopted to produce a functional ingredient such as texturized vegetable proteins, hydrolyzed vegetable protein, clean label protein concentrates, de‐flavored protein isolates, protein flour, and grits.

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Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

342

136

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“…Yellow pea proteins are made up of albumin (10-20%) and globulin (70-80% of the total seed protein) (Acquah et al, 2020). Albumins (∼5-80 kDa, 2S) are water-soluble metabolic proteins and can be mainly classified into enzymes, enzyme inhibitors and lectins (Barac, Pesic, Stanojevic, Kostic, & Bivolarevic, 2015;Djoullah, Husson, & Saurel, 2018;Lan et al, 2018) Although albumins contain high amounts of tryptophan, lysine, threonine, and methionine compared to globulins, which is more interesting from the nutritional point of view, globulins offer more opportunities for obtaining functional ingredients. Globulin, salt-soluble storage proteins, can be further divided based on their sedimentation coefficients into legumin (∼300-400 kDa, 11S), vicilin (∼150-170 kDa, 7S) and convicilin (∼70 kDa, 7S) (Bogahawaththa et al, 2019;Gao et al, 2020).…”

Section: Structurementioning

confidence: 99%

Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages.

Boukid

Rosell

Castellari

2021

Trends in Food Science & Technology

195

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Background: Pea (Pisum sativum) proteins are emerging as a popular alternative to those conventional (deriving from animal and soy) due to their high protein content with interesting functionality, sustainability, availability, affordability and hypo-allergenicity. This popularity has been parallel to an intensive research from protein isolation to their applications. Pea protein ingredients can be obtained through wet extraction, dry fractionation or more recently mild fractionation. As such, commercial pea proteins ingredients include flour (20-25% protein), concentrate (50-75% protein), and isolate (>80% protein). Beside protein content, these ingredients differ in their chemical composition, thereby affecting their functionality. Scope and Approach:In this perspective, this review offers the lastest update on essential knowledge for developing innovative food and beverages using pea proteins through emphasizing the production and the characteristics of pea proteins, addressing the efficiency of pea proteins as functional ingredients in foodstuffs making, and discussing the challenges encountered for pea protein popularization. Key Findings and Conclusions:Current research indicates the importance of developing extraction and drying technologies to reach target techno-functional and organoleptic attributes of pea proteins. A better modulation of processing steps can enable designing high-quality pea protein rich food and beverage.

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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.…”

mentioning

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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Gelation behaviors of denaturated pea albumin and globulin fractions during transglutaminase treatment

Cited by 65 publications

References 29 publications

Modification of plant proteins for improved functionality: A review

Modification of plant proteins for improved functionality: A review

Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages.

High pressure structuring of pea protein concentrates

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