Enzymatically Hydrolyzed Wheat Gluten as a Foaming Agent in Food: Incorporation in a Meringue Recipe as a Proof‐of‐Concept

Wouters, Arno G.B.; Rombouts, Ine; Fierens, Ellen; Brijs, Kristof; Delcour, Jan A.

doi:10.1111/1750-3841.14283

Cited by 28 publications

(26 citation statements)

References 47 publications

(79 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“… a Data are from multiple sources: (Arntfield, Murphy, & Ross, 2018; Boye, Zare, & Pletch, 2010; Cho, Jung, Auh, & Lee, 2017; Elzoghby, Samy, & Elgindy, 2012; Farzana, Mohajan, Saha, Hossain, & Haque, 2017; Grasso, Pintado, Pérez‐Jiménez, Ruiz‐Capillas, & Herrero, 2020; Gumus, Decker, & McClements, 2017; Krintiras, Diaz, Van Der Goot, Stankiewicz, & Stefanidis, 2016; Mohammed et al., 2018; Nguyen, Bhandari, Cichero, & Prakash, 2015; Pereira, Zhou, & Zhang, 2016; Pietsch et al., 2017; Wang, Gulati, Santra, Rose, & Zhang, 2018; Wouters, Rombouts, Fierens, Brijs, & Delcour, 2018; Xiao, Wang, Gonzalez, & Huang, 2016; Yoshie‐Stark, Wada, & Wäsche, 2008); Singh, Kumar, Sabapathy, & Bawa, 2008; Akharume, Santra, & Adedeji, 2020; Bainy, Tosh, Corredig, Poysa, & Woodrow, 2008; Chandi, & Sogi, 2007; Houde, Khodaei, Benkerroum, & Karboune, 2018; Katayama & Wilson, 2008; Ladjal‐Ettoumi, Boudries, Chibane, & Romero, 2016; Liu, Cao, Ren, Wang, & Zhang, 2019; Nwachukwu & Aluko, 2019; Schmiele, Felisberto, Clerici, & Chang, 2017; Taghdir et al., 2017; Wang, Wang, Wang, & Chen, 2016; Yalçın, Çelik, & İbanoğlu, 2008). …”

Section: Introductionmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

317

136

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

317

136

View full text Add to dashboard Cite

show abstract

“…An example of this is the successful (partial) replacement of egg white by WG hydrolysates in meringue recipes. 5 Amyloid fibrils (AFs) are protein structures which hold much promise for improving the techno-functional properties of food proteins. 6 This structure is also exploited by different organisms in Nature (e.g., Curli protein from Escherichia coli and protein Pmel17 involved in mammalian melanin synthesis) and has potential to be used as building blocks for bio-based materials.…”

Section: ■ Introductionmentioning

confidence: 99%

“…In that way, it can contribute to the increased use of plant proteins in food systems. An example of this is the successful (partial) replacement of egg white by WG hydrolysates in meringue recipes …”

Section: Introductionmentioning

confidence: 99%

Heating Wheat Gluten Promotes the Formation of Amyloid-like Fibrils

et al. 2021

Self Cite

View full text Add to dashboard Cite

Amyloid fibrils (AFs) are highly ordered nanofibers composed of proteins rich in β-sheet structures. In this study, the impact of heating conditions relevant in food processing on AF formation of wheat gluten (WG) was investigated. Unheated and heated WG samples were treated with proteinase K and trypsin to solubilize the nonfibrillated protein, while protein fibrils were extracted with 0.05 M sodium phosphate buffer (pH 7.0) from the undissolved fraction obtained by the same enzymatic treatment. Conditions (i.e., heating at 78° for 22 h) resembling those in slow cooking induced the formation of straight fibrils (ca. 700 nm in length), whereas boiling WG for at least 15 min resulted in longer straight fibrils (ca. 1–2 μm in length). The latter showed the typical green birefringence of AFs when stained with Congo red. Their X-ray fiber diffraction patterns showed the typical reflection (4.7 Å) for inter-β-strand spacing. These results combined with those of Fourier transform infrared and thioflavin T spectroscopy measurements validated the identification of β-rich amyloid-like fibrils (ALFs) in dispersions of boiled WG. Boiling for at least 15 min converted approximately 0.1–0.5% of WG proteins into ALFs, suggesting that they can be present in heat-treated WG-containing food products and that food-relevant heating conditions have the potential to induce protein fibrillation.

show abstract

“…9 In addition, hydrolysis of gluten enhances its solubility in aqueous media, which creates opportunities for a whole array of additional applications. 16 One route to the creation of novel applications is the formation of fibrils from gluten hydrolysates. Such hydrolysates have been prepared by incubating gluten with trypsin for two weeks at 37 °C and pH 8.0 under continuous gentle stirring.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Aqueous dispersions of wheat gluten can form ALFs by exposing them to conditions similar to those in slow cooking . In addition, hydrolysis of gluten enhances its solubility in aqueous media, which creates opportunities for a whole array of additional applications . One route to the creation of novel applications is the formation of fibrils from gluten hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Hydrothermal Treatments Cause Wheat Gluten-Derived Peptides to Form Amyloid-like Fibrils

Lambrecht

Monge-Morera

Godefroidt

et al. 2021

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Formation of amyloid fibrils (i.e. protein structures containing a compact core of ordered β-sheet structures) from food proteins can improve their techno-functional properties. Wheat gluten is the most consumed cereal protein by humans and extensively present in food and feed systems. Hydrolysis of wheat gluten increases the solubility of its proteins and brings new opportunities for value creation. In this study, the formation of amyloid-like fibrils (ALFs) from wheat gluten peptides (WGPs) under food relevant processing conditions was investigated. Different hydrothermal treatments were tested to maximize the formation of straight ALFs from WGPs. Thioflavin T (ThT) fluorescence measurements and transmission electron microscopy (TEM) were used to study the extent of fibrillation and the morphology of the fibrils, respectively. First, the formation of fibrils by heating solutions of tryptic WGPs [degrees of hydrolysis 2.0% (DH 2) or 6.0% (DH 6)] was optimized using a response surface design. WGP solutions were incubated at different pH, times and temperatures. DH 6 WGPs had a higher propensity for fibrillation than did DH 2 WGPs. Heating DH 6 WGPs at 2.0% (w/v) for 38 hours at 85 °C and pH 7.0 resulted in optimal fibrillation. Secondly, trypsin, chymotrypsin, thermolysin, papain and proteinase K were used to produce different DH 6 WGPs. After enzyme inactivation and subsequent heating at optimal fibrillation conditions, chymotrypsin and proteinase K DH 6 WGPs produced small worm-like fibrils whereas fibrils prepared from trypsin DH 6 WGPs were long and straight. The surface hydrophobicity of the peptides was key for fibrillation. Thirdly, peptides from the wheat gluten components gliadin and glutenin fractions formed smaller and worm-like fibrils than did WGPs. Thus, peptides of both gluten protein fractions jointly contribute in gluten fibrillation.

show abstract

Enzymatically Hydrolyzed Wheat Gluten as a Foaming Agent in Food: Incorporation in a Meringue Recipe as a Proof‐of‐Concept

Cited by 28 publications

References 47 publications

Modification of plant proteins for improved functionality: A review

Modification of plant proteins for improved functionality: A review

Heating Wheat Gluten Promotes the Formation of Amyloid-like Fibrils

Hydrothermal Treatments Cause Wheat Gluten-Derived Peptides to Form Amyloid-like Fibrils

Contact Info

Product

Resources

About