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Kutzli, I.; Gibis, M. Plant Protein Glycation. Encyclopedia. Available online: (accessed on 20 April 2024).
Kutzli I, Gibis M. Plant Protein Glycation. Encyclopedia. Available at: Accessed April 20, 2024.
Kutzli, Ines, Monika Gibis. "Plant Protein Glycation" Encyclopedia, (accessed April 20, 2024).
Kutzli, I., & Gibis, M. (2021, March 02). Plant Protein Glycation. In Encyclopedia.
Kutzli, Ines and Monika Gibis. "Plant Protein Glycation." Encyclopedia. Web. 02 March, 2021.
Plant Protein Glycation

Plant proteins are being considered to become the most important protein source of the future, and to do so, they must be able to replace the animal-derived proteins currently in use as techno-functional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the techno-functional characteristics of these proteins without the involvement of potentially toxic chemicals.

Plant Proteins Glycation Maillard reaction Food Ingredients Application Protein-Polysaccharide Conjugate Techno-Functionality

1. Introduction

A rising consumer demand for more natural and sustainable products has caused the food, cosmetic, and pharmaceutical sectors to increasingly develop and use plant-based ingredients to replace animal-based ones. This trend toward the use of sustainable and natural ingredients with “clean labels” is especially pronounced in food and beverage formulations and has led to the creation of a global market that is expected to be worth USD 47.5 billion by 2023 [1]. Besides their nutritional value, proteins are generally regarded as natural ingredients with valuable technological functionalities that can improve the texture and stability of many foods [2]. However, despite the current consumer demand for plant-based foods, a significant number of plant proteins are still underutilized in food preparations because their poor techno-functional properties limit their applicability and effectiveness in formulations [3]. Another common problem is the high allergenicity of many plant proteins, such as the ones derived from soy, wheat, and nuts [4], and the fact that many plant proteins contain antinutritional factors, such as several types of proteinase inhibitors that can hinder human digestion [5][6]. Moreover, the use of proteins as ingredients is generally hindered by their susceptibility to structural changes during processing steps (e.g., temperature/pressure treatment, change of pH/ionic strength), which can affect their techno-functionality [7].

To overcome these limitations associated with the use of proteins as techno-functional food ingredients, several modification approaches exist. These include chemical, physical, or enzymatic modification of the protein’s structure, as well as the addition of further synergistically acting ingredients [8]. Among these approaches, chemical and enzymatic methods have been shown to be very effective at improving the solubility, emulsifying, foaming, and gelling properties of food proteins [9][10][11]. However, most chemical approaches require the excessive use of toxic reagents and might produce harmful byproducts [12]. This greatly reduces the applicability of these approaches for the food industry. Thus, one of the most promising methods to improve the techno-functional properties of proteins is their glycation with carbohydrates under the influence of heat via the first step of the Maillard reaction. The Maillard reaction, as first described by Louis-Camille Maillard [13], involves a series of non-enzymatic reactions between the free amino groups of a protein and the carbonyl functions of a reducing carbohydrates. Since the Maillard reaction is a natural and spontaneously occurring process in food that does not require additional chemicals, it is superior to other chemical modification methods.

Over the past three decades, research has shown that glycation with carbohydrates via the Maillard reaction under the influence of heat can improve many of the techno-functional properties of food proteins [14][15][16][17]. Most of this research so far has been focused on animal-derived proteins, especially milk proteins such as whey proteins and caseins [18][19]. However, with climate change as the defining issue of our time, and faced with pressure to transition toward more environmentally sustainable practices, interest in studying the influence of glycation on the properties of plant-derived proteins has increased. 

2. Functional Properties and Potential Applications of Glycated Plant Proteins

2.1. Emulsifiers

The performance of glycated plant proteins as emulsifiers is their most extensively studied techno-functional property. Numerous studies have evaluated the emulsifying activity index and the emulsion stability index of the glycated proteins compared to the proteins before glycation [20][21][22]. In addition, the resistance of these emulsions against extrinsic factors such as heat treatments, salt addition, pH changes, or freezing–thawing has been evaluated [23][24][25].

Glycation of proteins indirectly improves their emulsifying properties by enhancing their solubility and mobility and providing added stability against extrinsic influences in aqueous solutions such as pH shifts or addition of salts [26][27]. In addition to electrostatic repulsion, emulsions formulated with glycated proteins also provide steric repulsion due to the added carbohydrate moiety. Upon adsorption, the carbohydrate part of the molecule is anchored at the interface between oil and water by the amphiphilic protein part and is exposed to the aqueous phase due to its hydrophilicity, where it physically hinders van der Waals attraction between oil droplets, especially at pH values close to the isoelectric point where electrostatic repulsion is low [26][28]. The thicker the interfacial layer, the better the resistance of oil droplets to aggregation and coalescence during storage and under the influence of mechanical stress and high shear forces (e.g., during unit operations such as mixing and pumping) [29][30][31]. Wong et al. [32] demonstrated that deamidated wheat protein glycated with dextran forms thicker interfacial layers than adsorbed protein alone. The conjugated wheat protein provided enhanced steric stabilization of emulsions under acidic pH conditions. Zhang et al. [33] showed that emulsions stabilized by soy protein isolate–maltodextrin conjugates exhibited high storage stability after two months at room temperature, especially at pH values around the isoelectric point of the protein, compared to emulsions stabilized with soy protein isolate only. In their study on canola protein isolate glycated with gum, Pirestani et al. [34] showed that conjugate-stabilized emulsions had smaller mean droplet sizes and lower creaming indices compared to emulsions stabilized by canola protein isolate or a mixture of the two polymers.

Beneficial effects of the glycation on emulsion stability were observed particularly if the pH was near the isoelectric point or after heat treatments. Protein–carbohydrate conjugates therefore have a high potential to be used as emulsifiers in transparent protein beverage formulations that have a low pH value or require heat treatment [35].

Moreover, protein-stabilized oil-in-water emulsions have been developed and widely used as delivery systems of hydrophobic bioactive compounds in food applications. Besides the positive effects on physical emulsion stability, glycation results in further beneficial properties for the use of glycated plant proteins as encapsulation agents (see 2.4).

2.2. Foaming

Like the emulsifying properties of a protein, its foaming properties also depend on its interfacial properties. Proteins adsorb to the air–water interface and stabilize the foam bubbles by electrostatic and steric repulsive forces [36]. Foaming properties are often represented by the foaming capacity and foam stability. High water solubility is a prerequisite of the protein to serve as a good foam stabilizer. Thus, the beneficial effects of glycation also positively impact its foaming properties [37]. Increased solubility upon glycation is attributed to an increased hydrophilicity and enhanced hydrogen-bonding capacity of the protein due to the covalent attachment of hydrophilic carbohydrates and the modification of the protein net charge, contributing to greater repulsion between protein molecules [38][26]. Further factors that influence the foaming properties of a protein are its molecular structure and flexibility [39].

Wen et al. [40] showed that glycation of soy protein isolate with lentinan by wet heating enhanced its foaming capacity and foam stability. This effect was even further promoted by using ultrasound-assisted wet heating since it enhanced the degree of glycation, which led to greater improvement of solubility, an increase in the random structure of the protein, as well as an increase of viscosity [40]. The foam stability of rice protein isolate could be increased by up to 2.74 times upon its glycation with dextran, depending on the ratio of protein to polysaccharide used. The improvement was ascribed to the increased solubility of the rice protein–dextran conjugate [41]. Further studies demonstrate a positive impact of glycation on the foaming properties of gluten–fructose conjugates [42] and fava bean protein–maltodextrin conjugates [43].

A potential application for these glycated proteins is foamable plant-based dairy alternatives, in which they might help to create foams high in volume and stability as a clean-label ingredient.

2.3. Films

An increasing interest in biodegradable packaging, e.g., for food products, has drawn attention to natural biopolymers such as proteins to develop biodegradable films. Additionally, these safe and edible films were studied for the delivery of bioactive compounds [44][45]. Films from plant proteins are the most attractive candidates due to their environmental sustainability [46]. However, compared to synthetic films, protein-based films have lower tensile-strength, elongation, and water-resistance properties due to their hydrophilic nature [47]. Because of this, the commercial application of protein films is not yet possible. Thus, protein modification or the addition of crosslinking agents are being studied.

One safe and effective modification method for the improvement of film properties is the glycation or crosslinking of proteins with carbohydrates [38]. A study by Liu et al. [46] showed that the glycation of peanut protein isolate with xylose led to films with a 77% increase in tensile strength, a 67% elongation increase, and a solubility decrease from 96.6% to 43.4% compared to peanut protein isolate films. These enhanced mechanical properties and water resistance could be correlated with the increased protein surface hydrophobicity and sulfhydryl group content with the addition upon glycation with xylose [46]. Positive effects on the mechanical properties were also reported for films made from peanut protein glycated with gum arabic [48] and soy protein glycated with glucomannan [49]. The importance of optimizing the degree of glycation to achieve the optimal outcome was demonstrated for films from wild almond protein. Grafting the protein with gum arabic for up to six days increased the tensile strength and the elongation of the films, while longer reaction times showed adverse effects [50].

2.4. Encapsulation

Most bioactive compounds are very sensitive to high temperatures, high salt concentrations, extreme pH values, and the presence of oxygen. In addition, many of them are restricted in their applicability by their limited water or oil solubility. To overcome these limitations, encapsulation systems in which bioactive compounds are entrapped by biomacromolecules in the form of emulsions, films, gels, or beads were developed [51].

Since glycated plant proteins show high solubility, excellent emulsification activity, and stability (see 2.1), as well as antioxidant properties, their use in the encapsulation of bioactive materials has attracted interest. Simultaneous increases in emulsifying properties and antioxidant activity upon glycation were observed for partially hydrolyzed soy protein isolate with maltodextrin [52], pea protein isolate with gum arabic [25], the soluble fraction of pea protein isolate with dextran [53], walnut protein isolate with glucose [54], and partially hydrolyzed black bean protein isolate with glucose [55]. These findings could be useful in the future development of encapsulation systems for hydrophobic, oxidation-sensitive compounds.

The improved stability of encapsulation systems with glycated plant proteins against external influences such as thermal treatments, extreme pH, and ionic salts are also useful in the encapsulation of bioactive compounds susceptible to gastric digestion. An example is the encapsulation of the essential oil citral. Due to its chemical instability and tendency to undergo changes during processing, storage, and gastric digestion, its application as antimicrobial agent is limited [56]. When citral was encapsulated in emulsions stabilized by soy protein isolate glycated with soy-soluble polysaccharide, outstanding physical stability after heat treatment and during the simulation of gastric digestion was observed [57][56]. The improvement of emulsion stability, and hence the controlled release of citral, was ascribed to the protection of soy protein against pancreatin digestion and the steric stabilization of emulsion droplets, both being a consequence of the glycation of soy protein isolate [57]. In another study, the glycation of soy protein isolate with gum arabic led to improved emulsifying properties. The glycated proteins were used as emulsifier and wall material for the encapsulation of tomato oleoresin, a lycopene-rich material, by spray-drying. These particles could protect the lycopene from being released in the stomach and degrading during storage [58]. Soy protein–carrageenan conjugates were also able to protect Bifidobacterium longum encapsulated by spray-drying from freeze-drying during storage, simulated gastric digestion, and pasteurization [59].


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Subjects: Plant Sciences
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