Impact of deamidation on gliadin-based nanoparticle formation and curcumin encapsulation

Wang, Yongquan; Yan, Wenjia; Lin, Rui; Jia, Xin; Cheng, Yongqiang

doi:10.1016/j.jfoodeng.2019.04.020

Cited by 40 publications

(19 citation statements)

References 26 publications

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“…A number of different preparation methods have been developed, with the most suitable one depending on the nature of the proteins. For example, protein nanoparticles can be formed from hydrophobic proteins, such as zein or gliadin, using an antisolvent precipitation method [ 29 ]. In this method, the hydrophobic proteins are first dissolved within a good solvent, such as a concentrated ethanol solution.…”

Section: Types Of Food Nanoparticlesmentioning

confidence: 99%

Recent Advances in the Gastrointestinal Fate of Organic and Inorganic Nanoparticles in Foods

Zhou

McClements

2022

Nanomaterials

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Inorganic or organic nanoparticles are often incorporated into foods to enhance their quality, stability, nutrition, or safety. When they pass through the gastrointestinal environment, the properties of these nanoparticles are altered, which impacts their biological effects and potential toxicity. Consequently, there is a need to understand how different kinds of nanoparticles behave within the gastrointestinal tract. In this article, the current understanding of the gastrointestinal fate of nanoparticles in foods is reviewed. Initially, the fundamental physicochemical and structural properties of nanoparticles are discussed, including their compositions, sizes, shapes, and surface chemistries. Then, the impact of food matrix effects and gastrointestinal environments on the fate of ingested nanoparticles is discussed. In particular, the influence of nanoparticle properties on food digestion and nutraceutical bioavailability is highlighted. Finally, future research directions are highlighted that will enable the successful utilization of nanotechnology in foods while also ensuring they are safe.

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Section: Types Of Food Nanoparticlesmentioning

confidence: 99%

Recent Advances in the Gastrointestinal Fate of Organic and Inorganic Nanoparticles in Foods

Zhou

McClements

2022

Nanomaterials

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“…Protein unfolding can expose hydrophobic residues, which generally increases the hydrophobicity (H 0 ) of deamidated proteins (Figure 4). The increase in hydrophobicity has been demonstrated in deamidated wheat gluten catalyzed by either HCl or organic acids (Cui et al, 2013;He et al, 2019;Liao et al, 2010a), deamidated wheat gliadin catalyzed by tartaric acid (Wang et al, 2019b), and deamidated glutelin of A. trifoliata var. australis seeds catalyzed by malic acid or citric acid (Lei et al, 2015).…”

Section: Chemical Deamidationmentioning

confidence: 99%

“…However, the excessively high degree of deamidation by longer reaction times or higher heating temperatures may lead to a significant decrease in the surface hydrophobicity. This is because excessive deamidation can cause the reassociation and aggregation of unfolded proteins or short peptides by hydrophobic/electrostatic forces or disulfide bonds (Lei et al, 2015;Liao et al, 2016a;Wang et al, 2019b;Zhao et al, 2010Zhao et al, , 2011.…”

Section: Chemical Deamidationmentioning

confidence: 99%

Protein deamidation to produce processable ingredients and engineered colloids for emerging food applications

Chen

Luo

et al. 2021

Comp Rev Food Sci Food Safe

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With the ever‐increasing demands for functional and sustainable foods from the general public, there is currently a paradigm shift in the food industry toward the production of novel protein‐based diet. Food scientists are therefore motivated to search for natural protein sources and innovative technologies to modify their chemical structure for desirable functionality and thus utilization. Deamidation is a viable, efficient, and attractive approach for modifying proteins owing to its ease of operating, specificity, and cost‐effective processes. Over the past three decades, the knowledge of protein deamidation for food applications has evolved drastically, including the development of novel approaches for deamidation, such as protein‐glutaminase and ion exchange resin, and their practices in new protein substrate. Thanks to deamidation, enhanced functionalities of food proteins from cereals, legumes, milk, oil seeds and others, and thereby their processabilities as food ingredients have been achieved. Moreover, deamidated proteins have been used to fabricate engineered food colloids, including self‐assembled protein particles, protein–metallic complexes, and protein–carbohydrate complexes, which have demonstrated tailored physicochemical properties to modulate oral perception, improve gastrointestinal digestion and bioavailability, and protect and/or deliver bioactive nutrients. Novel bioactivity, altered digestibility, and varied allergenicity of deamidated proteins are increasingly recognized. Therefore, deamidated proteins with novel techno‐functional and biological properties hold both promise and challenges for future food applications, and a comprehensive review on this area is critically needed to update our knowledge and provide a better understanding on the protein deamidation and its emerging applications.

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“…They include hydrogen bonds, van der Waals forces, and hydrophobic effects (Le Bourvellec & Renard, 2012). Zein (Hu, Wang, Fernandez, & Luo, 2016) and gliadins (Wang, Yan, Li, Jia, & Cheng, 2019e) are commonly used to prepare prolamin/polyphenol complexes. Prolamin‐based complexes with tannic acid (TA) (Zou et al., 2019), curcumin (Patel, Hu, Tiwari, & Velikov, 2010), and resveratrol (Qiu, Wang, Wang, & Teng, 2017) have been extensively studied.…”

Section: Prolamin/polyphenol Binary Complexesmentioning

confidence: 99%

“…Other interactions, such as ionic bonds between the positively charged groups of prolamins and the negatively charged hydroxyl groups of polyphenols, play minor roles (Le Bourvellec & Renard, 2012). Gliadin couples with curcumin through noncovalent hydrophobic interactions and hydrogen bonding, which increases the stability and bioavailability of curcumin (Wang, Yan, et al., 2019). Approximately 21 protein segments of zein hydrolysate (ZH) bind to one molecule of TA, suggesting that ZH “wraps around” TA and confirming that the complex formation between ZH and TA is driven by noncovalent interactions (Wang et al., 2016).…”

Section: Prolamin/polyphenol Binary Complexesmentioning

confidence: 99%

Prolamin‐based complexes: Structure design and food‐related applications

Song

Sun

Gul

et al. 2021

Comp Rev Food Sci Food Safe

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Prolamins are a group of safe food additives that are biocompatible, biodegradable, and sustainable. Zein, gliadin, kafirin, and hordein are common prolamins that have been extensively studied, particularly as these form colloidal particles because of their amphiphilic properties. Prolamin‐based binary/ternary complexes, which have stable physicochemical properties and superior functionality, are formed by combining prolamins with polysaccharides, polyphenols, water‐soluble proteins, and surfactants. Although the combination of prolamins with other components has received attention, the relationship between the structural design of prolamin‐based complexes and their functionalities remains uncertain. This review discusses the production methods of prolamin‐based complexes, the factors influencing their structural characteristics, and their applications in the food industry. Further studies are needed to elucidate the structure–function relationships between prolamins and other biopolymers, as well as the toxicological effects of these complexes in food.

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Impact of deamidation on gliadin-based nanoparticle formation and curcumin encapsulation

Cited by 40 publications

References 26 publications

Recent Advances in the Gastrointestinal Fate of Organic and Inorganic Nanoparticles in Foods

Recent Advances in the Gastrointestinal Fate of Organic and Inorganic Nanoparticles in Foods

Protein deamidation to produce processable ingredients and engineered colloids for emerging food applications

Prolamin‐based complexes: Structure design and food‐related applications

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